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Myosin Light Chain Kinase and the Onset of Labour in Humans
Author(s) -
Moore Frances,
Bernal Andrés López
Publication year - 2001
Publication title -
experimental physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.925
H-Index - 101
eISSN - 1469-445X
pISSN - 0958-0670
DOI - 10.1113/eph8602188
Subject(s) - myosin light chain kinase , myosin , immunoglobulin light chain , medicine , endocrinology , chemistry , microbiology and biotechnology , cardiology , biology , immunology , antibody
Myosin light chain kinase (MLCK) is essential for myometrial contractions induced by calcium‐mobilizing agonists. From the gene of vertebrate smooth muscle/non‐muscle MLCK there are at least four proteins expressed. We have found that both a > 200 and a 137 kDa MLCK are equally expressed in human non‐pregnant (NP) and term pregnant (P) uterine smooth muscle and confirmed that 19 kDa telokin (TK) is only expressed in P myometrium. In addition, we have observed that a MLCK immunogen at ∼ 60 kDa is only expressed in NP myometrium, suggesting that its expression is inhibited during normal pregnancy in a hormonally dependent manner. However, when we compared pregnant myometrium from patients delivered preterm (PT) (< 34 weeks gestation), but not in labour (NIL), with PT patients in labour (IL) we found that PT(IL) samples expressed the ∼ 60 kDa MLCK immunogen and thus displayed a NP phenotype whereas PT(NIL) samples did not express the protein and retained a pregnant phenotype. We hypothesize that the novel ∼ 60 kDa MLCK immunogen contributes to the aberrent contractility associated with preterm labour.

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