Serveur d'exploration sur les relations entre la France et l'Australie

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A colostrum trypsin inhibitor gene expressed in the Cape fur seal mammary gland during lactation.

Identifieur interne : 002476 ( Main/Exploration ); précédent : 002475; suivant : 002477

A colostrum trypsin inhibitor gene expressed in the Cape fur seal mammary gland during lactation.

Auteurs : Elizabeth A. Pharo [Australie] ; Kylie N. Cane [Australie] ; Julia Mccoey [Australie] ; Ashley M. Buckle [Australie] ; W H Oosthuizen [Afrique du Sud] ; Christophe Guinet [France] ; John P Y. Arnould [Australie]

Source :

RBID : pubmed:26639991

Descripteurs français

English descriptors

Abstract

The colostrum trypsin inhibitor (CTI) gene and transcript were cloned from the Cape fur seal mammary gland and CTI identified by in silico analysis of the Pacific walrus and polar bear genomes (Order Carnivora), and in marine and terrestrial mammals of the Orders Cetartiodactyla (yak, whales, camel) and Perissodactyla (white rhinoceros). Unexpectedly, Weddell seal CTI was predicted to be a pseudogene. Cape fur seal CTI was expressed in the mammary gland of a pregnant multiparous seal, but not in a seal in its first pregnancy. While bovine CTI is expressed for 24-48 h postpartum (pp) and secreted in colostrum only, Cape fur seal CTI was detected for at least 2-3 months pp while the mother was suckling its young on-shore. Furthermore, CTI was expressed in the mammary gland of only one of the lactating seals that was foraging at-sea. The expression of β-casein (CSN2) and β-lactoglobulin II (LGB2), but not CTI in the second lactating seal foraging at-sea suggested that CTI may be intermittently expressed during lactation. Cape fur seal and walrus CTI encode putative small, secreted, N-glycosylated proteins with a single Kunitz/bovine pancreatic trypsin inhibitor (BPTI) domain indicative of serine protease inhibition. Mature Cape fur seal CTI shares 92% sequence identity with Pacific walrus CTI, but only 35% identity with BPTI. Structural homology modelling of Cape fur seal CTI and Pacific walrus trypsin based on the model of the second Kunitz domain of human tissue factor pathway inhibitor (TFPI) and porcine trypsin (Protein Data Bank: 1TFX) confirmed that CTI inhibits trypsin in a canonical fashion. Therefore, pinniped CTI may be critical for preventing the proteolytic degradation of immunoglobulins that are passively transferred from mother to young via colostrum and milk.

DOI: 10.1016/j.gene.2015.11.042
PubMed: 26639991


Affiliations:


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Le document en format XML

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<term>Animals</term>
<term>Cattle</term>
<term>Colostrum (enzymology)</term>
<term>Computer Simulation</term>
<term>Female</term>
<term>Fur Seals (genetics)</term>
<term>Fur Seals (metabolism)</term>
<term>Gene Expression</term>
<term>Lactation (metabolism)</term>
<term>Mammals (metabolism)</term>
<term>Mammary Glands, Animal (metabolism)</term>
<term>Pregnancy</term>
<term>Structural Homology, Protein</term>
<term>Swine</term>
<term>Trypsin (metabolism)</term>
<term>Trypsin Inhibitors (chemistry)</term>
<term>Trypsin Inhibitors (metabolism)</term>
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<term>Animaux</term>
<term>Bovins</term>
<term>Colostrum (enzymologie)</term>
<term>Expression des gènes</term>
<term>Femelle</term>
<term>Glandes mammaires animales (métabolisme)</term>
<term>Grossesse</term>
<term>Inhibiteurs trypsiques ()</term>
<term>Inhibiteurs trypsiques (métabolisme)</term>
<term>Lactation (métabolisme)</term>
<term>Mammifères (métabolisme)</term>
<term>Otaries à fourrure (génétique)</term>
<term>Otaries à fourrure (métabolisme)</term>
<term>Similitude structurale de protéines</term>
<term>Simulation numérique</term>
<term>Suidae</term>
<term>Trypsine (métabolisme)</term>
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<term>Trypsin Inhibitors</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en">
<term>Trypsin</term>
<term>Trypsin Inhibitors</term>
</keywords>
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<term>Colostrum</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en">
<term>Colostrum</term>
</keywords>
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<term>Fur Seals</term>
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<term>Otaries à fourrure</term>
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<term>Fur Seals</term>
<term>Lactation</term>
<term>Mammals</term>
<term>Mammary Glands, Animal</term>
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<term>Glandes mammaires animales</term>
<term>Inhibiteurs trypsiques</term>
<term>Lactation</term>
<term>Mammifères</term>
<term>Otaries à fourrure</term>
<term>Trypsine</term>
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<term>Cattle</term>
<term>Computer Simulation</term>
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<term>Expression des gènes</term>
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<term>Grossesse</term>
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<div type="abstract" xml:lang="en">The colostrum trypsin inhibitor (CTI) gene and transcript were cloned from the Cape fur seal mammary gland and CTI identified by in silico analysis of the Pacific walrus and polar bear genomes (Order Carnivora), and in marine and terrestrial mammals of the Orders Cetartiodactyla (yak, whales, camel) and Perissodactyla (white rhinoceros). Unexpectedly, Weddell seal CTI was predicted to be a pseudogene. Cape fur seal CTI was expressed in the mammary gland of a pregnant multiparous seal, but not in a seal in its first pregnancy. While bovine CTI is expressed for 24-48 h postpartum (pp) and secreted in colostrum only, Cape fur seal CTI was detected for at least 2-3 months pp while the mother was suckling its young on-shore. Furthermore, CTI was expressed in the mammary gland of only one of the lactating seals that was foraging at-sea. The expression of β-casein (CSN2) and β-lactoglobulin II (LGB2), but not CTI in the second lactating seal foraging at-sea suggested that CTI may be intermittently expressed during lactation. Cape fur seal and walrus CTI encode putative small, secreted, N-glycosylated proteins with a single Kunitz/bovine pancreatic trypsin inhibitor (BPTI) domain indicative of serine protease inhibition. Mature Cape fur seal CTI shares 92% sequence identity with Pacific walrus CTI, but only 35% identity with BPTI. Structural homology modelling of Cape fur seal CTI and Pacific walrus trypsin based on the model of the second Kunitz domain of human tissue factor pathway inhibitor (TFPI) and porcine trypsin (Protein Data Bank: 1TFX) confirmed that CTI inhibits trypsin in a canonical fashion. Therefore, pinniped CTI may be critical for preventing the proteolytic degradation of immunoglobulins that are passively transferred from mother to young via colostrum and milk.</div>
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