Studies on proteolysis of protein kinase C with calpain I and II.

Studies on proteolysis of protein kinase C with calpain I and II. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Studies on proteolysis of protein kinase C with calpain I and II. Abstract Text:

Earlier reports from this laboratory have shown that protein kinase C (PKC) is cleaved with Ca2(+)-dependent neutral protease (calpain) I or II to produce a catalytically active fragment, and that calpain I, which is active in the micromolar range of Ca2+, may react preferentially with the active form of PKC that is associated with membranes. Subsequently, PKC is shown to exist as a large family of multiple subspecies with subtle individual characteristics. Three types of PKC designated types I, II, and III are purified from rat brain cytosol, which are shown to correspond to the cDNA clones gamma, beta, and alpha, respectively. The aim of the present study was to characterize the proteolysis of each PKC subspecies with calpain I and II. All types of PKC (82 kDa) were converted to two major fragments: a 47-49-kDa catalytic and a 36-kDa regulatory fragments by the cleavage with either calpain I or II. Analysis of the NH2-terminal sequence of the resulting catalytic fragments indicated that both calpain I and II cleaved at one or two specific sites in the variable region (V3) of each PKC molecule of which structure was clearly different among PKC subspecies. From kinetic studies, the cleavage of PKC subspecies with calpain I, and to a lesser extent, with calpain II (active in the millimolar range of Ca2+), was remarkably enhanced by the simultaneous presence of phospholipid and diacylglycerol or phorbol ester, suggesting that the active forms of PKC subspecies were the preferred targets for proteolysis. Whereas, stimulatory abilities of the lipids were variable among PKC subspecies and inactive form of type I PKC was cleaved with calpain I at a significant rate. Quantitative analysis with a fixed amount of calpain under comparable conditions showed that the susceptibilities of the PKC subspecies were distinctly different one another; the relative rates of cleavage of types I, II, and III PKC with calpain I and II were approximately 100:16:2 and 100:48:23, respectively. These results indicated that within the cell various PKC subspecies might be cleaved at different rates under different physiological conditions.

Studies on proteolysis of protein kinase C with calpain I and II. Publishing Authors By Initials

For similar animals: chordata: vertebrates: mammals: rodentia: muridae: murinae: rats research abstracts see: animals: chordata: vertebrates: mammals: rodentia: muridae: murinae: rats research

PUBMED ID PMID:

MEDLINE DATE:

Studies on proteolysis of protein kinase C with calpain I and II. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: The Kobe journal of medical sciences

VOLUME: 36

Page Numbers: 55-69

Journal Abbreviation: Kobe J Med Sci

ISSN: 0023-2513

DAY: 8

MONTH: Apr

YEAR: 1990

Studies on proteolysis of protein kinase C with calpain I and II. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 413531

Studies on proteolysis of protein kinase C with calpain I and II. Keywords Mesh Terms:

KEYWORDS: Rats

MESH TERMS: physiology

Chemical & Substance for Abstract: Studies on proteolysis of protein kinase C with calpain I and II. Information

Substance Name: Calpain

Registry Number: EC 3.4.22.-

Grant and Affiliation Information for Studies on proteolysis of protein kinase C with calpain I and II.

AFFILIATION: Department of Anaesthesiology and Biochemistry, Kobe University School of Medicine.

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: Kobe J Med Sci

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Studies on proteolysis of protein kinase C with calpain I and II Related Publications

• 'Freezing' of the calcium-regulated structures of gizzard thin filaments by glutaraldehyde.
• A quantitative enzyme-linked immunosorbent assay for Dermatophagoides pteronyssinus-specific immunoglobulin G.
• Changes in myosin isozymes during development of chicken breast muscle.
• Depth EEG in mutant epileptic E1 mice: demonstration of secondary generalization of the seizure from the hippocampus.
• Induction of proepicardial marker gene expression by the liver bud.
• Morphological characteristics of the scalp far-field potentials evoked by median nerve stimulation in infants and children.
• Pharmacokinetics of beclomethasone dipropionate in an hydrofluoroalkane-134a propellant system in Japanese children with bronchial asthma.
• RecR forms a ring-like tetramer that encircles dsDNA by forming a complex with RecF.
• Separation and identification of Drosophila myosin light chains.
• Studies on proteolysis of protein kinase C with calpain I and II.
• The process of displacing the single-stranded DNA-binding protein from single-stranded DNA by RecO and RecR proteins.