Results 161 to 170 of about 4,652 (211)

Immunoblotting for Calpastatin Expression

open access: yes, 2019
Immunoblotting is a procedure routinely used to analyze calpastatin expression. However, immunoblotting alone may not be adequate for this task, since calpastatin isoforms can vary by tissue, can be modified by partial digestion, and can undergo posttranslational modifications.
Averna, Monica, De Tullio, Roberta
openaire   +4 more sources

Isolation of Endogenous Calpastatin

open access: yes, 2019
We here describe the purification of calpastatin from human erythrocytes. When calpastatin is purified from tissues, it is necessary to measure its inhibitory activity against calpain in the presence of Ca2+ to specifically identify the protein. Thus, the purification steps necessary to obtain the inhibitor protein were originally designed to obtain ...
De Tullio, Roberta, Averna, Monica
openaire   +4 more sources

Immunoaffinity purification of calpastatin and calpastatin constructs

BBA - Proteins and Proteomics, 2002
It has been difficult to purify calpastatin without using a step involving heating to 90-100 degrees C. Preparations of calpastatin obtained after heating often contain several polypeptides that have been ascribed to proteolytic degradation. Because calpastatin is highly susceptible to proteolytic degradation and several different calpastatin isoforms ...
Valery F Thompson, Darrel E Goll
exaly   +3 more sources

Production and Purification of Recombinant Calpastatin

open access: yes, 2019
The production of recombinant calpastatin in E. coli has become an efficient tool to obtain discrete amounts of a specific calpastatin species that can be present concomitantly with other calpastatin fragments/forms in the same tissue or cell type in a given condition.
De Tullio, Roberta, Averna, Monica
openaire   +4 more sources

Correlation between a novel calpastatin biosensor and traditional calpastatin assay techniques

Biosensors and Bioelectronics, 2008
An optical fiber biosensor to detect calpastatin has been investigated as a preliminary step in developing tenderness detection instrumentation. Longissimus dorsi samples were taken from beef carcasses (n=21) at 0, 24, 36 and 48h postmortem. Muscle homogenates were assayed for calpastatin activity using traditional methods and an optical fiber ...
Sheila A Grant, C L Lorenzen
exaly   +3 more sources

Expression of calpastatin isoforms in muscle and functionality of multiple calpastatin promoters

open access: yesArchives of Biochemistry and Biophysics, 2004
Calpastatin is the specific endogenous inhibitor of calpain proteinase that is encoded by a single gene. Transient transfection assays in both a non-fusing skeletal muscle and non-muscle cell-line demonstrated that the putative porcine calpastatin promoter regions 5' to exons 1xa, 1xb, and 1u were functional.
Tim, Parr   +5 more
openaire   +3 more sources

Calpastatin level in spontaneously hypertensive rats

open access: yesBiochemical and Biophysical Research Communications, 1991
We studied calpastatin activity in erythrocytes of Milan hypertensive and prehypertensive rats, in their normotensive controls, in F1 and F2 hybrids, and in two inbred strains derived from F2, one hypertensive and the other normotensive. Our results show that the decrease in calpastatin activity observed in Milan hypertensive rats was not caused by ...
L. Soldati   +6 more
openaire   +5 more sources

Cardiac high molecular weight calmodulin-binding protein is homologous to calpastatin I and calpastatin II

Biochemical and Biophysical Research Communications, 2008
Calpastatin is an endogenous inhibitor of calpain, which has been implicated in various physiological and pathological processes. In the present study we determined the molecular and inhibitory properties of HMWCaMBP, calpastatin I, and calpastatin II. Western blot analysis with antibodies raised against either full length HMWCaMBP or internal peptides
Nisha Singh   +2 more
exaly   +3 more sources

Calpain–calpastatin system and cancer progression

Biological Reviews, 2021
ABSTRACTThe calpain system is required by many important physiological processes, including the cell cycle, cytoskeleton remodelling, cellular proliferation, migration, cancer cell invasion, metastasis, survival, autophagy, apoptosis and signalling, as well as the pathogenesis of a wide range of disorders, in which it may function to promote ...
Hong Nian, Binyun Ma
openaire   +2 more sources

Interaction of calpastatin with calpain: a review

Biological Chemistry, 2004
Calpastatin is a multiheaded inhibitor capable of inhibiting more than one calpain molecule. Each inhibitory domain of calpastatin has three subdomains, A, B, and C; A binds to domain IV and C binds to domain VI of the calpains. Crystallographic evidence shows that binding of C to domain VI involves hydrophobic interactions at a site near the first EF ...
Amanda, Wendt   +2 more
openaire   +2 more sources

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