Postmortem proteolysis and calpain/calpastatin activity in callipyge and normal lamb biceps femoris during extended postmortem storage.

Geesink, G.H.; Koohmaraie, M.

doi:10.2527/1999.7761490x

Cited by 141 publications

(104 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The muscle of Callipyge sheep has increased calpastatin (Geesink & Koohmaraie, 1999;Duckett, Snowder & Cockett, 2000), reduced breaks in the I-band region during post mortem aging (Taylor & Koohmaraie, 1998) and no change in collagen cross-linking (Field, McCormick, Brown, Hinds & Snowder, 1996) Solomon, Long, Eastridge & Carpenter, 1995;Clare, Jackson, Miller, Elliot & Ramsey, 1997;Shackelford, Wheeler & Koohmaraie, 1997Duckett, Klein, Dodson & Snowder, 1998).…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Genetic and environmental effects on meat quality

Warner¹,

et al. 2010

View full text Add to dashboard Cite

In order for livestock industries to consistently produce high quality meat, there must be an understanding of the factors that cause quality to vary, as well as the contribution of genetics. A brief overview of meat tenderness is presented to understand how genotype and environment may interact to influence this trait.Essentially, meat tenderness is determined from the contribution of connective tissue, sarcomere length determined pre-rigor and rate of proteolysis during ageing, as well as contributions from intramuscular fat and post-mortem energy metabolism. The influence of mutations in myostatin, the callipyge gene, the Carwell or ribe eye muscle gene as well as the calpain system on meat tenderness is presented. Specific examples of interactions between the production or processing environment and genetics are presented for both sheep and cattle. The day-to-day variation in tenderness is evident across experiments and this variation needs to be controlled in order to consistently produce tender meat.

show abstract

Section: Accepted Manuscriptmentioning

confidence: 99%

Genetic and environmental effects on meat quality

Warner¹,

et al. 2010

View full text Add to dashboard Cite

show abstract

“…Similar to calpains, calpastatin is found in muscle fibers mainly at the Z-line region of myofibrils (14). Geesink and Koohmaraie (10) showed that increased calpastatin levels inhibit the activity and degradation rate of cytoskeletal structural proteins of the muscle fibers. These results indicate that the calpain system is largely responsible for degradation of structural proteins, thus determining final meat quality (11).…”

Section: Water Content and Drip Loss Of Muscle Fibersmentioning

confidence: 99%

Integrin degradation during postmortem cold storage and the level of drip loss in pork

Górska

Wojtysiak

2017

Medycyna Weterynaryjna

View full text Add to dashboard Cite

SummaryIntegrins are a family of transmembrane adhesion proteins. An integrin molecule is composed of two subunits called α and β, each of which has a large extracellular domain, a transmembrane fragment, and a short cytoplasmic sequence. The main function of integrin is to bind extracellular matrix proteins and the skeletal muscle cell membrane. In addition, integrin as a membrane receptor is involved in signal transduction and cell response to microenvironmental signals, by relaying information about the structure and composition of the cell environment. Postmortem integrin degradation has been the subject of several studies, mainly in pork, where the mechanisms of postmortem integrin degradation are not completely understood. Therefore, the aim of the study was to present current knowledge on the role of integrin in postmortem drip loss in pork.Research to date has shown that postmortem integrin degradation could contribute to the formation of drip channels between the cell body and cell membrane of muscle fibers, which increases the drip loss from pork.

show abstract

“…The interaction of pH, temperature and post mortem time affect the biochemical dynamics of early post mortem meat and hence the rate of proteolysis (25). Geesink and Koohmaraie have described how post mortem degradation of myofibrillar proteins is involved in meat tenderness and in particular the degradation pattern of contractile proteins (26).…”

Section: Meat Proteomicsmentioning

confidence: 99%