* 150210

LACTOTRANSFERRIN; LTF


Alternative titles; symbols

LACTOFERRIN; LF


HGNC Approved Gene Symbol: LTF

Cytogenetic location: 3p21.31     Genomic coordinates (GRCh38): 3:46,435,645-46,485,234 (from NCBI)


TEXT

Description

Lactoferrin is an iron-binding glycoprotein of the transferrin (TF; 190000) family that is expressed in most biologic fluids and is a major component of mammals' innate immune system (Legrand et al., 2008).


Cloning and Expression

Yang et al. (1983) cloned human cDNA for lactotransferrin.

Powell and Ogden (1990) reported the nucleotide sequence of human lactoferrin cDNA. The deduced protein contains 709 amino acids, including a 17-amino acid putative signal peptide.

In a review, Legrand et al. (2008) stated that the mature LF protein contains 690 amino acids and is highly basic. It has a positively charged N terminus that shares 40% sequence identity with the C terminus. LF shares 60% amino acid identity with transferrin (TF; 190000).


Biochemical Features

Crystal Structure

Anderson et al. (1987) determined the 3-dimensional structure of human lactoferrin at 3.2 angstrom resolution.


Gene Function

Lactoferrin is widely distributed in exocrine secretions, notably milk, and is an important component of leukocytes. It has strong bacteriostatic properties. These result from its avidity for iron, depriving bacteria of iron essential for growth. It may also protect cells from free radical damage by binding potentially catalytic free iron (summary by Anderson et al., 1987).

Campbell (1982) presented evidence that lactoferrin shares binding to a specific receptor of alveolar macrophages with 2 other neutrophil granule glycoproteins, cathepsin G (116830) and leukocyte elastase (130130).

Bezault et al. (1994) found that Lf inhibited solid tumor growth and tumor metastasis in mice. Natural killer cells appeared to be involved in Lf antimetastatic activity in mouse tumor models.

Haemophilus influenzae is a major cause of otitis media and other respiratory tract disease in children. The pathogenesis of the disease begins with colonization of the upper respiratory mucosa, a process that involves evasion of local immune mechanisms and adherence to epithelial cells. Several studies demonstrated that human milk is protective against H. influenzae colonization and disease. Qiu et al. (1998) examined the effect of human milk on 2 autotransported proteins of H. influenzae that are presumed to facilitate colonization: IgA1 protease and Hap adhesin. They found that human milk lactoferrin efficiently extracted the IgA1 protease preprotein from the bacterial outer membrane. In addition, lactoferrin specifically degraded the Hap adhesin and abolished Hap-mediated adherence. The results suggested that human milk lactoferrin attenuates the pathogenic potential of H. influenzae by selectively inactivating IgA1 protease and Hap, thereby interfering with colonization. They suggested that future studies should examine the therapeutic potential of lactoferrin, perhaps as a supplement in infant formulas.

Human T-cell leukemia virus-1 (HTLV-1) causes T-cell leukemia and lymphoma and is clustered in certain geographic areas. Like HIV-1 infection, HTLV-1 infection can be transmitted vertically through breast milk. Refraining from breast feeding was found to efficiently block mother-to-infant transmission in southwestern Japan. Moriuchi and Moriuchi (2001) observed a dose-dependent enhancement of HTLV-1 replication by transactivating the viral long terminal repeat in cells stimulated with human or bovine lactoferrin. Lactoferrin also accelerated transmission to uninfected cord blood mononuclear cells. Moriuchi and Moriuchi (2001) confirmed that lactoferrin inhibits HIV-1 replication and showed that it does so by nonspecifically blocking viral fusion to cells.

Singh et al. (2002) hypothesized that the innate immune system possesses specific activity to protect against biofilm infections and demonstrated that lactoferrin, a ubiquitous and abundant constituent of human external secretions, blocks biofilm development by the opportunistic pathogen Pseudomonas aeruginosa. This occurs at lactoferrin concentrations below those that kill or prevent growth. By chelating iron, lactoferrin stimulates twitching, a specialized form of surface motility, causing the bacteria to wander across the surface instead of forming cell clusters and biofilms. Singh et al. (2002) concluded that their findings reveal a specific antibiofilm defense mechanism acting at a critical juncture in biofilm development.

In a review of LF structure and function, Legrand et al. (2008) stated that LF downregulates proinflammatory cytokine and reactive oxygen species production. A number of pathogens have lactoferrin-binding molecules, and LF has antimicrobial activity, partly due to its metal and ion chelation properties.

Using clarified saliva and biotinylated human herpesvirus-8 (HHV-8), which is also known as Kaposi sarcoma (148000)-associated herpesvirus (KSHV), Grange et al. (2005) detected binding to the 78-kD LF protein. Binding did not require glycosylation. Approximately 8% of HHV-8-uninfected individuals tested expressed a form of LF that was not recognized by HHV-8. Endoprotease cleavage of native LF generated a nonglycosylated 8-kD peptide corresponding to amino acids 606 to 679 in the C-terminal region of LF that bound HHV-8. Grange et al. (2005) concluded that LF in saliva is a ligand for HHV-8 and possibly a carrier of viral particles.

Grange et al. (2012) showed that LF or the 8-kD LF C-terminal peptide enhanced KSHV infection of a human epithelial cell line and primary human foreskin fibroblasts.


Gene Structure

Kim et al. (1998) determined that the LF gene contains 17 exons and spans 24.5 kb.


Mapping

Mouse cDNA for lactotransferrin was used by Naylor et al. (1987) to map the gene in mouse and in man. Southern blot analysis of somatic cell hybrid DNA and in situ hybridization placed the LTF gene in the 3q21-q23 region, where transferrin is also located (McCombs et al., 1988). Naylor et al. (1987) and Teng et al. (1987) found, furthermore, that in the mouse LTF sequences are located on chromosome 9, where the transferrin gene is also located in that species. Because of the high degree of homology between transferrin and lactoferrin (about 80% at the amino acid level), it is possible that these 2 genes are very close to each other.

By FISH, Kim et al. (1998) mapped the LF gene to chromosome 3p21.3.


Animal Model

Ward et al. (2003) developed lactoferrin-null mice and found them to be viable and fertile. They developed normally and displayed no overt abnormalities. Lactoferrin was not required for intestinal iron uptake, and relatively normal iron parameters were observed in lactoferrin-null mice. In situ hybridization of wildtype animals demonstrated that lactoferrin is not expressed in the postnatal or adult intestine. Ward et al. (2003) concluded that the functional role of this protein in the intestine during the postnatal period is likely imparted by maternal milk-derived lactoferrin.


Molecular Genetics

Velliyagounder et al. (2003) characterized a lys/arg polymorphism at position 29 in human LF that results from a SNP in exon 1. LF variants containing lys29 or arg29 exhibited nearly identical iron-binding and iron-releasing activities and equivalent bactericidal activities against a strain of the gram-negative bacterium Actinobacillus actinomycetemcomitans. However, LF containing lys29 exhibited significantly greater bactericidal activity against the gram-negative species Streptococcus mutans and Streptococcus mitis than did LF containing arg29. In addition, LF with lys29 stimulated bovine tracheal epithelial cells to synthesize much higher levels of tracheal antimicrobial peptide (TAP; 602560) than did LF with arg29. Lys29 and arg29 had allele frequencies of 24% and 76%, respectively, among 17 healthy humans, and 72% and 28%, respectively, among 9 patients with localized juvenile periodontitis.


See Also:

REFERENCES

  1. Anderson, B. F., Baker, H. M., Dodson, E. J., Norris, G. E., Rumball, S. V., Waters, J. M., Baker, E. N. Structure of human lactoferrin at 3.2-angstrom resolution. Proc. Nat. Acad. Sci. 84: 1769-1773, 1987. [PubMed: 3470756, related citations] [Full Text]

  2. Bezault, J., Bhimani, R., Wiprovnick, J., Furmanski, P. Human lactoferrin inhibits growth of solid tumors and development of experimental metastases in mice. Cancer Res. 54: 2310-2312, 1994. [PubMed: 8162571, related citations]

  3. Campbell, E. J. Human leukocyte elastase, cathepsin G, and lactoferrin: family of neutrophil granule glycoproteins that bind to an alveolar macrophage receptor. Proc. Nat. Acad. Sci. 79: 6941-6945, 1982. [PubMed: 6960357, related citations] [Full Text]

  4. Grange, P. A., Gressier, L., Williams, J. F., Dyson, O. F., Akula, S. M., Dupin, N. Cloning a human saliva-derived peptide for preventing KSHV transmission. (Letter) J. Invest. Derm. 132: 1733-1735, 2012. [PubMed: 22377758, related citations] [Full Text]

  5. Grange, P. A., Marcelin, A.-G., Calvez, V., Chauvel, C., Escande, J.-P., Dupin, N. Salivary lactoferrin is recognized by the human herpesvirus-8. J. Invest. Derm. 124: 1249-1258, 2005. [PubMed: 15955101, related citations] [Full Text]

  6. Kim, S. J., Yu, D.-Y., Pak, K.-W., Jeong, S., Kim, S.-W., Lee, K.-K. Structure of the human lactoferrin gene and its chromosomal localization. Molec. Cells 8: 663-668, 1998. [PubMed: 9895117, related citations]

  7. Legrand, D., Pierce, A., Elass, E., Carpentier, M., Mariller, C., Mazurier, J. Lactoferrin structure and functions. Adv. Exp. Med. Biol. 606: 163-194, 2008. [PubMed: 18183929, related citations] [Full Text]

  8. McCombs, J. L., Teng, C. T., Pentecost, B. T., Magnuson, V. L., Moore, C. M., McGill, J. R. Chromosomal localization of human lactotransferrin gene (LTF) by in situ hybridization. Cytogenet. Cell Genet. 47: 16-17, 1988. [PubMed: 3356163, related citations] [Full Text]

  9. Moriuchi, M., Moriuchi, H. A milk protein lactoferrin enhances human T cell leukemia virus type I and suppresses HIV-1 infection. J. Immun. 166: 4231-4236, 2001. [PubMed: 11238676, related citations] [Full Text]

  10. Naylor, S. L., Marshall, A., Solomon, A., McGill, J. R., McCombs, J., Magnuson, V. L., Moore, C. M., Lalley, P. A., Pentecost, B. T., Teng, C. Lactoferrin maps to human chromosome 3(q21-q23) and mouse chromosome 9. (Abstract) Cytogenet. Cell Genet. 46: 669 only, 1987.

  11. Powell, M. J., Ogden, J. E. Nucleotide sequence of human lactoferrin cDNA. Nucleic Acids Res. 18: 4013 only, 1990. [PubMed: 2374734, related citations] [Full Text]

  12. Qiu, J., Hendrixson, D. R., Baker, E. N., Murphy, T. F., St. Geme, J. W., III, Plaut, A. G. Human milk lactoferrin inactivates two putative colonization factors expressed by Haemophilus influenzae. Proc. Nat. Acad. Sci. 95: 12641-12646, 1998. [PubMed: 9770539, images, related citations] [Full Text]

  13. Rado, T. A., Wei, X., Benz, E. J., Jr. Isolation of lactoferrin cDNA from a human myeloid library and expression of mRNA during normal and leukemic myelopoiesis. Blood 70: 989-993, 1987. [PubMed: 3477300, related citations]

  14. Singh, P. K., Parsek, M. R., Greenberg, E. P., Welsh, M. J. A component of innate immunity prevents bacterial biofilm development. Nature 417: 552-555, 2002. [PubMed: 12037568, related citations] [Full Text]

  15. Teng, C. T., Pentecost, B. T., Marshall, A., Solomon, A., Bowman, B. H., Lalley, P. A., Naylor, S. L. Assignment of the lactotransferrin gene to human chromosome 3 and to mouse chromosome 9. Somat. Cell Molec. Genet. 13: 689-693, 1987. [PubMed: 3478818, related citations] [Full Text]

  16. Velliyagounder, K., Kaplan, J. B., Furgang, D., Legarda, D., Diamond, G., Parkin, R. E., Fine, D. H. One of two human lactoferrin variants exhibits increased antibacterial and transcriptional activation activities and is associated with localized juvenile periodontitis. Infect. Immun. 71: 6141-6147, 2003. [PubMed: 14573629, images, related citations] [Full Text]

  17. Ward, P. P., Mendoza-Meneses, M., Cunningham, G. A., Conneely, O. M. Iron status in mice carrying a targeted disruption of lactoferrin. Molec. Cell. Biol. 23: 178-185, 2003. [PubMed: 12482971, images, related citations] [Full Text]

  18. Yang, F., Lum, J., Baldwin, W. D., Brune, J. L., van Bragt, P., Bowman, B. H. Genetic analysis of human iron binding glycoproteins. (Abstract) Am. J. Hum. Genet. 35: 184A only, 1983.


Paul J. Converse - updated : 6/4/2012
Matthew B. Gross - updated : 7/9/2008
Paul J. Converse - updated : 5/27/2008
Patricia A. Hartz - updated : 2/27/2003
Ada Hamosh - updated : 5/28/2002
Paul J. Converse - updated : 4/30/2001
Victor A. McKusick - updated : 11/2/1998
Creation Date:
Victor A. McKusick : 6/2/1986
carol : 06/04/2018
carol : 06/01/2018
carol : 05/09/2014
mgross : 6/12/2012
terry : 6/4/2012
carol : 11/5/2009
mgross : 7/9/2008
terry : 5/27/2008
mgross : 4/25/2008
joanna : 4/25/2008
terry : 3/16/2005
mgross : 2/27/2003
alopez : 5/29/2002
terry : 5/28/2002
mgross : 4/30/2001
carol : 11/9/1998
terry : 11/2/1998
supermim : 3/16/1992
carol : 3/3/1992
carol : 11/8/1990
carol : 9/26/1990
supermim : 3/20/1990
ddp : 10/27/1989

* 150210

LACTOTRANSFERRIN; LTF


Alternative titles; symbols

LACTOFERRIN; LF


HGNC Approved Gene Symbol: LTF

Cytogenetic location: 3p21.31     Genomic coordinates (GRCh38): 3:46,435,645-46,485,234 (from NCBI)


TEXT

Description

Lactoferrin is an iron-binding glycoprotein of the transferrin (TF; 190000) family that is expressed in most biologic fluids and is a major component of mammals' innate immune system (Legrand et al., 2008).


Cloning and Expression

Yang et al. (1983) cloned human cDNA for lactotransferrin.

Powell and Ogden (1990) reported the nucleotide sequence of human lactoferrin cDNA. The deduced protein contains 709 amino acids, including a 17-amino acid putative signal peptide.

In a review, Legrand et al. (2008) stated that the mature LF protein contains 690 amino acids and is highly basic. It has a positively charged N terminus that shares 40% sequence identity with the C terminus. LF shares 60% amino acid identity with transferrin (TF; 190000).


Biochemical Features

Crystal Structure

Anderson et al. (1987) determined the 3-dimensional structure of human lactoferrin at 3.2 angstrom resolution.


Gene Function

Lactoferrin is widely distributed in exocrine secretions, notably milk, and is an important component of leukocytes. It has strong bacteriostatic properties. These result from its avidity for iron, depriving bacteria of iron essential for growth. It may also protect cells from free radical damage by binding potentially catalytic free iron (summary by Anderson et al., 1987).

Campbell (1982) presented evidence that lactoferrin shares binding to a specific receptor of alveolar macrophages with 2 other neutrophil granule glycoproteins, cathepsin G (116830) and leukocyte elastase (130130).

Bezault et al. (1994) found that Lf inhibited solid tumor growth and tumor metastasis in mice. Natural killer cells appeared to be involved in Lf antimetastatic activity in mouse tumor models.

Haemophilus influenzae is a major cause of otitis media and other respiratory tract disease in children. The pathogenesis of the disease begins with colonization of the upper respiratory mucosa, a process that involves evasion of local immune mechanisms and adherence to epithelial cells. Several studies demonstrated that human milk is protective against H. influenzae colonization and disease. Qiu et al. (1998) examined the effect of human milk on 2 autotransported proteins of H. influenzae that are presumed to facilitate colonization: IgA1 protease and Hap adhesin. They found that human milk lactoferrin efficiently extracted the IgA1 protease preprotein from the bacterial outer membrane. In addition, lactoferrin specifically degraded the Hap adhesin and abolished Hap-mediated adherence. The results suggested that human milk lactoferrin attenuates the pathogenic potential of H. influenzae by selectively inactivating IgA1 protease and Hap, thereby interfering with colonization. They suggested that future studies should examine the therapeutic potential of lactoferrin, perhaps as a supplement in infant formulas.

Human T-cell leukemia virus-1 (HTLV-1) causes T-cell leukemia and lymphoma and is clustered in certain geographic areas. Like HIV-1 infection, HTLV-1 infection can be transmitted vertically through breast milk. Refraining from breast feeding was found to efficiently block mother-to-infant transmission in southwestern Japan. Moriuchi and Moriuchi (2001) observed a dose-dependent enhancement of HTLV-1 replication by transactivating the viral long terminal repeat in cells stimulated with human or bovine lactoferrin. Lactoferrin also accelerated transmission to uninfected cord blood mononuclear cells. Moriuchi and Moriuchi (2001) confirmed that lactoferrin inhibits HIV-1 replication and showed that it does so by nonspecifically blocking viral fusion to cells.

Singh et al. (2002) hypothesized that the innate immune system possesses specific activity to protect against biofilm infections and demonstrated that lactoferrin, a ubiquitous and abundant constituent of human external secretions, blocks biofilm development by the opportunistic pathogen Pseudomonas aeruginosa. This occurs at lactoferrin concentrations below those that kill or prevent growth. By chelating iron, lactoferrin stimulates twitching, a specialized form of surface motility, causing the bacteria to wander across the surface instead of forming cell clusters and biofilms. Singh et al. (2002) concluded that their findings reveal a specific antibiofilm defense mechanism acting at a critical juncture in biofilm development.

In a review of LF structure and function, Legrand et al. (2008) stated that LF downregulates proinflammatory cytokine and reactive oxygen species production. A number of pathogens have lactoferrin-binding molecules, and LF has antimicrobial activity, partly due to its metal and ion chelation properties.

Using clarified saliva and biotinylated human herpesvirus-8 (HHV-8), which is also known as Kaposi sarcoma (148000)-associated herpesvirus (KSHV), Grange et al. (2005) detected binding to the 78-kD LF protein. Binding did not require glycosylation. Approximately 8% of HHV-8-uninfected individuals tested expressed a form of LF that was not recognized by HHV-8. Endoprotease cleavage of native LF generated a nonglycosylated 8-kD peptide corresponding to amino acids 606 to 679 in the C-terminal region of LF that bound HHV-8. Grange et al. (2005) concluded that LF in saliva is a ligand for HHV-8 and possibly a carrier of viral particles.

Grange et al. (2012) showed that LF or the 8-kD LF C-terminal peptide enhanced KSHV infection of a human epithelial cell line and primary human foreskin fibroblasts.


Gene Structure

Kim et al. (1998) determined that the LF gene contains 17 exons and spans 24.5 kb.


Mapping

Mouse cDNA for lactotransferrin was used by Naylor et al. (1987) to map the gene in mouse and in man. Southern blot analysis of somatic cell hybrid DNA and in situ hybridization placed the LTF gene in the 3q21-q23 region, where transferrin is also located (McCombs et al., 1988). Naylor et al. (1987) and Teng et al. (1987) found, furthermore, that in the mouse LTF sequences are located on chromosome 9, where the transferrin gene is also located in that species. Because of the high degree of homology between transferrin and lactoferrin (about 80% at the amino acid level), it is possible that these 2 genes are very close to each other.

By FISH, Kim et al. (1998) mapped the LF gene to chromosome 3p21.3.


Animal Model

Ward et al. (2003) developed lactoferrin-null mice and found them to be viable and fertile. They developed normally and displayed no overt abnormalities. Lactoferrin was not required for intestinal iron uptake, and relatively normal iron parameters were observed in lactoferrin-null mice. In situ hybridization of wildtype animals demonstrated that lactoferrin is not expressed in the postnatal or adult intestine. Ward et al. (2003) concluded that the functional role of this protein in the intestine during the postnatal period is likely imparted by maternal milk-derived lactoferrin.


Molecular Genetics

Velliyagounder et al. (2003) characterized a lys/arg polymorphism at position 29 in human LF that results from a SNP in exon 1. LF variants containing lys29 or arg29 exhibited nearly identical iron-binding and iron-releasing activities and equivalent bactericidal activities against a strain of the gram-negative bacterium Actinobacillus actinomycetemcomitans. However, LF containing lys29 exhibited significantly greater bactericidal activity against the gram-negative species Streptococcus mutans and Streptococcus mitis than did LF containing arg29. In addition, LF with lys29 stimulated bovine tracheal epithelial cells to synthesize much higher levels of tracheal antimicrobial peptide (TAP; 602560) than did LF with arg29. Lys29 and arg29 had allele frequencies of 24% and 76%, respectively, among 17 healthy humans, and 72% and 28%, respectively, among 9 patients with localized juvenile periodontitis.


See Also:

Rado et al. (1987)

REFERENCES

  1. Anderson, B. F., Baker, H. M., Dodson, E. J., Norris, G. E., Rumball, S. V., Waters, J. M., Baker, E. N. Structure of human lactoferrin at 3.2-angstrom resolution. Proc. Nat. Acad. Sci. 84: 1769-1773, 1987. [PubMed: 3470756] [Full Text: https://doi.org/10.1073/pnas.84.7.1769]

  2. Bezault, J., Bhimani, R., Wiprovnick, J., Furmanski, P. Human lactoferrin inhibits growth of solid tumors and development of experimental metastases in mice. Cancer Res. 54: 2310-2312, 1994. [PubMed: 8162571]

  3. Campbell, E. J. Human leukocyte elastase, cathepsin G, and lactoferrin: family of neutrophil granule glycoproteins that bind to an alveolar macrophage receptor. Proc. Nat. Acad. Sci. 79: 6941-6945, 1982. [PubMed: 6960357] [Full Text: https://doi.org/10.1073/pnas.79.22.6941]

  4. Grange, P. A., Gressier, L., Williams, J. F., Dyson, O. F., Akula, S. M., Dupin, N. Cloning a human saliva-derived peptide for preventing KSHV transmission. (Letter) J. Invest. Derm. 132: 1733-1735, 2012. [PubMed: 22377758] [Full Text: https://doi.org/10.1038/jid.2012.30]

  5. Grange, P. A., Marcelin, A.-G., Calvez, V., Chauvel, C., Escande, J.-P., Dupin, N. Salivary lactoferrin is recognized by the human herpesvirus-8. J. Invest. Derm. 124: 1249-1258, 2005. [PubMed: 15955101] [Full Text: https://doi.org/10.1111/j.0022-202X.2005.23756.x]

  6. Kim, S. J., Yu, D.-Y., Pak, K.-W., Jeong, S., Kim, S.-W., Lee, K.-K. Structure of the human lactoferrin gene and its chromosomal localization. Molec. Cells 8: 663-668, 1998. [PubMed: 9895117]

  7. Legrand, D., Pierce, A., Elass, E., Carpentier, M., Mariller, C., Mazurier, J. Lactoferrin structure and functions. Adv. Exp. Med. Biol. 606: 163-194, 2008. [PubMed: 18183929] [Full Text: https://doi.org/10.1007/978-0-387-74087-4_6]

  8. McCombs, J. L., Teng, C. T., Pentecost, B. T., Magnuson, V. L., Moore, C. M., McGill, J. R. Chromosomal localization of human lactotransferrin gene (LTF) by in situ hybridization. Cytogenet. Cell Genet. 47: 16-17, 1988. [PubMed: 3356163] [Full Text: https://doi.org/10.1159/000132496]

  9. Moriuchi, M., Moriuchi, H. A milk protein lactoferrin enhances human T cell leukemia virus type I and suppresses HIV-1 infection. J. Immun. 166: 4231-4236, 2001. [PubMed: 11238676] [Full Text: https://doi.org/10.4049/jimmunol.166.6.4231]

  10. Naylor, S. L., Marshall, A., Solomon, A., McGill, J. R., McCombs, J., Magnuson, V. L., Moore, C. M., Lalley, P. A., Pentecost, B. T., Teng, C. Lactoferrin maps to human chromosome 3(q21-q23) and mouse chromosome 9. (Abstract) Cytogenet. Cell Genet. 46: 669 only, 1987.

  11. Powell, M. J., Ogden, J. E. Nucleotide sequence of human lactoferrin cDNA. Nucleic Acids Res. 18: 4013 only, 1990. [PubMed: 2374734] [Full Text: https://doi.org/10.1093/nar/18.13.4013]

  12. Qiu, J., Hendrixson, D. R., Baker, E. N., Murphy, T. F., St. Geme, J. W., III, Plaut, A. G. Human milk lactoferrin inactivates two putative colonization factors expressed by Haemophilus influenzae. Proc. Nat. Acad. Sci. 95: 12641-12646, 1998. [PubMed: 9770539] [Full Text: https://doi.org/10.1073/pnas.95.21.12641]

  13. Rado, T. A., Wei, X., Benz, E. J., Jr. Isolation of lactoferrin cDNA from a human myeloid library and expression of mRNA during normal and leukemic myelopoiesis. Blood 70: 989-993, 1987. [PubMed: 3477300]

  14. Singh, P. K., Parsek, M. R., Greenberg, E. P., Welsh, M. J. A component of innate immunity prevents bacterial biofilm development. Nature 417: 552-555, 2002. [PubMed: 12037568] [Full Text: https://doi.org/10.1038/417552a]

  15. Teng, C. T., Pentecost, B. T., Marshall, A., Solomon, A., Bowman, B. H., Lalley, P. A., Naylor, S. L. Assignment of the lactotransferrin gene to human chromosome 3 and to mouse chromosome 9. Somat. Cell Molec. Genet. 13: 689-693, 1987. [PubMed: 3478818] [Full Text: https://doi.org/10.1007/BF01534490]

  16. Velliyagounder, K., Kaplan, J. B., Furgang, D., Legarda, D., Diamond, G., Parkin, R. E., Fine, D. H. One of two human lactoferrin variants exhibits increased antibacterial and transcriptional activation activities and is associated with localized juvenile periodontitis. Infect. Immun. 71: 6141-6147, 2003. [PubMed: 14573629] [Full Text: https://doi.org/10.1128/IAI.71.11.6141-6147.2003]

  17. Ward, P. P., Mendoza-Meneses, M., Cunningham, G. A., Conneely, O. M. Iron status in mice carrying a targeted disruption of lactoferrin. Molec. Cell. Biol. 23: 178-185, 2003. [PubMed: 12482971] [Full Text: https://doi.org/10.1128/MCB.23.1.178-185.2003]

  18. Yang, F., Lum, J., Baldwin, W. D., Brune, J. L., van Bragt, P., Bowman, B. H. Genetic analysis of human iron binding glycoproteins. (Abstract) Am. J. Hum. Genet. 35: 184A only, 1983.


Contributors:
Paul J. Converse - updated : 6/4/2012
Matthew B. Gross - updated : 7/9/2008
Paul J. Converse - updated : 5/27/2008
Patricia A. Hartz - updated : 2/27/2003
Ada Hamosh - updated : 5/28/2002
Paul J. Converse - updated : 4/30/2001
Victor A. McKusick - updated : 11/2/1998

Creation Date:
Victor A. McKusick : 6/2/1986

Edit History:
carol : 06/04/2018
carol : 06/01/2018
carol : 05/09/2014
mgross : 6/12/2012
terry : 6/4/2012
carol : 11/5/2009
mgross : 7/9/2008
terry : 5/27/2008
mgross : 4/25/2008
joanna : 4/25/2008
terry : 3/16/2005
mgross : 2/27/2003
alopez : 5/29/2002
terry : 5/28/2002
mgross : 4/30/2001
carol : 11/9/1998
terry : 11/2/1998
supermim : 3/16/1992
carol : 3/3/1992
carol : 11/8/1990
carol : 9/26/1990
supermim : 3/20/1990
ddp : 10/27/1989