1998
DOI: 10.1016/s0014-5793(98)01475-6
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A new intracellular serine protease inhibitor expressed in the rat pituitary gland complexes with granzyme B

Abstract: We have cloned a novel serpin (raPIT5a) from a rat pituitary cDNA library which is structurally related to members of the ovalbumin subfamily of serine protease inhibitors. This new cDNA encodes a 374-amino acid protein, designated raPIT5a. raPIT5a was expressed in specific cells in the intermediate and anterior lobes of the pituitary. Recombinant raPIT5a was not secreted suggesting raPIT5a functions to inhibit intracellular proteases. Recombinant raPIT5a formed an SDS-stable complex with human granzyme B, a s… Show more

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Cited by 8 publications
(6 citation statements)
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“…Thus, we can infer that the overexpression of G6PD in PMFs contributes to their proliferative advantage over MF‐HSCs. The protein “similar to serine protease inhibitor 6”, also named raPIT5a, the equivalent of rat/mouse serine protease inhibitor 6 and of human PI 9 27, is a granzyme B inhibitor 28. Granzyme B is secreted by natural killer (NK) cells and causes cell death.…”
Section: Discussionmentioning
confidence: 99%
“…Thus, we can infer that the overexpression of G6PD in PMFs contributes to their proliferative advantage over MF‐HSCs. The protein “similar to serine protease inhibitor 6”, also named raPIT5a, the equivalent of rat/mouse serine protease inhibitor 6 and of human PI 9 27, is a granzyme B inhibitor 28. Granzyme B is secreted by natural killer (NK) cells and causes cell death.…”
Section: Discussionmentioning
confidence: 99%
“…(1) PAI-2, a macrophage-derived serpin, protects against TNF-induced apoptosis in addition to its role in regulating extracellular urokinase, (2) PI-9, an intracellular serpin present in T lymphocytes, inhibits granzyme B and protects the cell against perforin and granzyme Bmediated killing, and (3) raPIT5a, a serpin that seems to regulate granzyme B-mediated apoptosis in the pituitary gland [35,36,43,44].…”
Section: Discussionmentioning
confidence: 99%
“…The functions of these proteins remain unclear but may involve the stabilization of extracellular matrices (Huang et al, 1993), and more recently, in the case of the larger family, a role in inhibiting apoptosis (Hill et al, 1998; Stahler and Roemer, 1998). ITI heavy chains are expressed abundantly in the liver and contain a putative binding site for hyaluronic acid (HA).…”
Section: Introductionmentioning
confidence: 99%