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Differential Processing of High-Molecular-Weight Kininogen during Normal Pregnancy.

08:00 EDT 14th August 2019 | BioPortfolio

Summary of "Differential Processing of High-Molecular-Weight Kininogen during Normal Pregnancy."

Studies identified kininogen as a potential biomarker of preeclampsia, a major cause of adverse maternal outcomes. High-molecular-weight kininogen (HK) and its activated form (HKa) participate in numerous pathways associated with establishing and maintaining pregnancy. However, dynamic changes in HK and naturally occurring HK-derived peptides during natural course of pregnancy are largely unknown.

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This article was published in the following journal.

Name: Rapid communications in mass spectrometry : RCM
ISSN: 1097-0231
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Medical and Biotech [MESH] Definitions

Endogenous peptides present in most body fluids. Certain enzymes convert them to active KININS which are involved in inflammation, blood clotting, complement reactions, etc. Kininogens belong to the cystatin superfamily. They are cysteine proteinase inhibitors. HIGH-MOLECULAR-WEIGHT KININOGEN; (HMWK); is split by plasma kallikrein to produce BRADYKININ. LOW-MOLECULAR-WEIGHT KININOGEN; (LMWK); is split by tissue kallikrein to produce KALLIDIN.

A protein, molecular weight 50 kD, located in various normal tissues. Upon cleavage by KALLIKREINS, it forms KALLIDIN. Kallidin, in turn, is converted into BRADYKININ. (From Stedman, 25th ed)

A plasma protein, molecular weight of 110 kD, that normally exists in plasma in a 1:1 complex with PREKALLIKREIN. HMWK is split by plasma kallikrein to produce BRADYKININ. The complex is a cofactor in the activation of coagulation factor XII. The product of this reaction, XIIa, in turn activates prekallikrein to KALLIKREINS. (From Stedman, 26th ed)

Activated form of factor XI. In the intrinsic pathway, Factor XI is activated to XIa by factor XIIa in the presence of cofactor HMWK; (HIGH MOLECULAR WEIGHT KININOGEN). Factor XIa then activates factor IX to factor IXa in the presence of calcium.

A low-molecular-weight protein (minimum molecular weight 8000) which has the ability to inhibit trypsin as well as chymotrypsin at independent binding sites. It is characterized by a high cystine content and the absence of glycine.

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