Identification of a splice variant of neutrophil collagenase (MMP‐8)

FEBS Letters

Carozza, Marc¹  Rediske, John¹  Peppard, Jane¹  Qi, Jian-Shen¹  Klein, Melissa¹  Hu, Shou-Ih¹ 

[1]Department of Arthritis Biology, LSB3183, Novartis Institute for Biomedical Research, 556 Morris Avenue, Summit, NJ 07901, USA

关键词: Neutrophil collagenase;    MMP-8;    Alternative splicing;    In vitro translation;    Co-translational processing;    Autoactivation;   

DOI  :  10.1016/S0014-5793(98)01654-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have identified a splice variant of human neutrophil collagenase (MMP-8) transcript (MMP-8alt) that has a 91 bp insertion between codons for amino acid residues 34 and 35 of MMP-8 cDNA. This splice variant encodes an open reading frame for a 444 residue protein, lacking a secretory signal sequence. Our data suggested that, as opposed to the original MMP-8, the translation product of MMP-8alt is not a secreted protein; nevertheless, it is enzymatically active. Further studies aimed at identifying the physiological substrates of MMP-8alt protein may lead to uncover novel roles it plays in cellular physiology.

【 授权许可】

Unknown