Distribution Of Calpains Research Articles

Meat tenderness genetic polymorphisms occurrence and distribution in five Zebu breeds in Mexico

Background: The Zebu cattle are represented by a diverse group of breeds in Mexico. Traditionally these breeds have been associated with the tough beef characteristic. Validated genetic markers have the potential to be included in marker-assisted selection and management programs in order to improve traits such as beef tenderness. The incidence and distribution of Calpain and Calpastatin polymorphisms strongly associated with beef tenderness were estimated in registered cattle of five Zebu breeds in Mexico. Results: A low and in some cases null frequency of favorable C allele of CAPN316 was determined in all breeds. Conversely, a more equilibrated frequency in CAPN4751 and CAST loci was observed. Conclusions: Although the relatively low occurrence of favorable alleles in assessed loci may limit their use in selection programs, genotyping availability might be a practical and comprehensive tool for introgression programs by marker assisted selection and management as to improve meat tenderness of Zebu breeds. Normal 0 21 false false false ES-CL X-NONE X-NONE /* Style Definitions */ table.MsoNormalTable {mso-style-name:Tabla normal; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin-top:0cm; mso-para-margin-right:0cm; mso-para-margin-bottom:10.0pt; mso-para-margin-left:0cm; line-height:115%; mso-pagination:widow-orphan; font-size:11.0pt; font-family:Calibri,sans-serif; mso-ascii-font-family:Calibri; mso-ascii-theme-font:minor-latin; mso-hansi-font-family:Calibri; mso-hansi-theme-font:minor-latin; mso-ansi-language:ES-MX; mso-fareast-language:EN-US;}

ELF-MF transiently increases skeletal myoblast migration: Possible role of calpain system

Purpose: Cell migration is crucial for myogenesis since it is required for the alignment and fusion of myoblast. Ca2+ signals are involved in regulating myoblast migration and an extremely low frequency (ELF) magnetic field (MF) increases intracellular calcium levels in C2C12 myoblast. This study was aimed at investigating whether ELF-MF could affect myoblast migration. As calpains contribute to the regulation of myoblast motility, the effect of ELF-MF on μ- and m-calpain was also investigated.Materials and methods: The effect of ELF-MF (1 mT; 50 Hz) on C2C12 cell motility was observed by wound-healing assay. Protein expression of calpains, calpastatin, myristoylated alanine-rich C-kinase substrate (MARCKS) and vinculin were examined by Western blot analysis. Casein zymography and immunofluorescence analysis were carried out to evaluate, respectively, activity levels of calpains and intracellular distribution of calpains, calpastatin and actin.Results: Exposure to ELF-MF resulted in a transient but significant increase of myoblast migration. This stimulatory effect was associated with a marked increase of μ- and m-calpain activity followed by the concomitant variation in their subcellular localization. No significant changes in intracellular distribution and protein levels of calpastatin were detected. Finally, a significant decrease of MARCKS expression and modifications of actin dynamics were reported.Conclusions: This study clearly outlines an involvement of calpains in ELF-MF-mediated myoblast migration.

Calpain 10 gene single-nucleotide 44 polymorphism may have an influence on clinical and metabolic features in patients with polycystic ovary syndrome

This study was designed in order to examine the relationship between Calpain 10 [single-nucleotide polymorphism (SNP) 19,43,44,63] gene polymorphisms and clinical and hormonal characteristics in women with polycystic ovary syndrome (PCOS). One hundred and seven patients with PCOS and 114 healthy subjects were included in this study. Serum levels of sex steroids were measured for each individual. Insulin resistance (IR) was evaluated by the homeostasis model assessment (HOMA) and quantitative insulin-sensitivity check index (QUICKI) methods. Insulin and glucose responses to the oral glucose tolerance test (OGTT) were analyzed by calculating the areas under the curve for insulin (AUCI) and glucose by the trapezoidal methods.We used PCR and restriction fragment length polymorphism technique to examine Calpain 10 SNP 19, 43, 44, and 63 polymorphisms. Allele distribution of Calpain 10 SNP 44 gene polymorphism was observed as significantly different between the groups. Calpain 10 SNP 44 TC genotype was found to be increased in PCOS subjects (69.15%) compared to the control subjects (50%). However, when compared to control subjects, patients with PCOS had similar Calpain 10 SNP 19, Calpain 10 SNP 43, and SNP 63 gene polymorphisms. When compared with normal Calpain 10 gene SNP 44 allele in PCOS subjects, subjects with PCOS having Calpain 10 gene SNP 44 allele polymorphism had higher free testosterone, androstenedione, DHEA-S, and fasting insulin levels. Also, PCOS women with Calpain 10 gene SNP 44 allele polymorphism had high Ferriman-Gallwey (F-G) score, acne, prevalence of menstrual disturbances, waist-hip ratio, HOMA-IR, AUCI levels and low QUICKI levels. The findings show that Calpain 10 gene SNP 44 allele polymorphism may have a role in PCOS pathogenesis. However, larger-scale studies are needed in this field.

ORIGINAL ARTICLE: Role of μ‐Calpain in Human Decidua for Recurrent Miscarriage

Problem Earlier, we showed that calpain activated by increasing intracellular calcium ion concentration in endometrial cells, causes endometrial dysfunction for implantation and early pregnancy. In the present study, we investigated the existence and distribution of calpains, calpastatin, integrin β3 and α‐fodrin in decidua from patients with recurrent miscarriage.Method of study Deciduae were surgically collected from 29 patients with recurrent miscarriage and 20 healthy women with informed consent. Immunohistochemistry, sodium dodecyl sulphate–polyacrylamide gel electrophoresis, and western blot analysis were performed.Results Staining of μ‐calpain, m‐calpain, calpastatin, integrin β3 and α‐fodrin were observed in the cytoplasm of stromal and epithelial cells in decidua using immunohistochemistry. No significant differences were observed in staining patterns. Western blot analysis showed no significant differences in expression of m‐calpain, calpastatin and α‐fodrin, whereas μ‐calpain was significantly higher and integrin β3 was lower in subject.Conclusion The results suggest that cleavage of integrin β3 by μ‐calpain may have an adverse effect on the mechanism of early pregnancy.

Intracellular distribution and regulation of calpains in the thyroid gland.

We studied the distribution of calpains in various subcellular thyrocyte fractions and evaluated the possibility for direct activation of calpain localized in the plasma membrane by thyrotropin. Direct activation of calpain bound to the plasma membrane did not underlie transduction of the thyrotropin signal to Ca(2+)-dependent proteinases.

Immunohistochemical Distribution and Electron Microscopic Subcellular Localization of the Proteasome in the Rat CNS

The proteasome multicatalytic proteinase (MCP) is a 20S complex that plays a major role in nonlysosomal pathways of intracellular protein degradation. A polyclonal antibody against rat liver MCP was used to investigate the distribution of MCP in the CNS of the rat and its subcellular localization within the neurons. As expected, MCP immunoreactivity (MCP-IR) was distributed ubiquitously in the rat CNS but not homogeneously. The most intensely stained neurons were the pyramidal cortical neurons of layer 5 and the motor neurons of the ventral horn in the spinal cord, which show an intense nuclear and cytoplasmatic MCP-IR and clearly stained processes. Additionally, some populations of large neurons in the mesencephalon and brainstem also displayed a moderate MCP-IR in their perikarya. The vast majority of neurons in the remaining structures did not show a strong cytoplasmatic MCP-IR, but their nuclei displayed an intense MCP-IR. The subcellular localization also was studied by immunoelectron microscopy. MCP-IR was intense in the neuronal nuclei, and significant staining also was found in the cytoplasm, dendritic, and axonic processes (including some myelinated axons) and in synaptic boutons, as illustrated in the cerebellar cortex. The distribution of MCP in the rat CNS and its subcellular localization are discussed in relation to (1) the distribution of calpain, the other major nonlysosomal cellular protease, and (2) the possible role of MCP in the degradation of regulatory proteins and key transcription factors that are essential in many neuronal responses.

Distribution of calpains I and II in rat brain

Calpains I and II are calcium-dependent proteases that have been implicated in several aspects of brain function, including neurofilament turnover, Wallerian degeneration, and excitatory synaptic transmission. In this study, specific affinity-purified antibodies against each of the enzymes were used to determine their cellular distribution in rat brain. Differences between the two were found throughout the brain, with calpain I being located primarily in neurons, whereas calpain II was more prominent in glial cells. In myelinated axons, calpain II was present at low levels but calpain I was not detectable. In all brain areas, both enzymes were concentrated in cell bodies, with lesser amounts in neuronal and glial processes. Calpain I was only detectable proximally in dendrites and was not found in spiny branchlets of either pyramidal or Purkinje cells. These results suggest that calpain II is the likely form of the enzyme involved in calcium-activated proteolytic phenomena in axons. They do not support the existence of a role for calpain at excitatory axospinous synapses.

Reversed Distribution of Calpains and Calpastatin in Human Pituitary Gland and Selective Localization of Calpastatin in Adrenocorticotropin-Producing Cells as Demonstrated by Immunohistochemistry*

The immunohistochemical distribution of Ca2+-dependent cysteine proteinases (calpains I and II) and their endogenous inhibitor calpastatin in normal and adenomatous human pituitary tissue was studied using specific antibodies. The distributions of calpain and calpastatin were dissimilar in human pituitary gland, i.e. ACTH-immunoreactive cells were strongly positive for calpastatin and negative for calpains. PRL-, GH-, FSH-, and TSH-producing cells were negative for calpastatin, but moderately positive for calpains, especially for calpain II, the high Ca2+-requiring form of the enzyme. Similar results were found in pituitary adenoma tissue. These findings indicate that each type of cells producing a specific hormone is equipped with a different balance of the enzyme-inhibitor system involved in the Ca2+-dependent degradation of intracellular proteins.

Distribution of calpain I, an enzyme associated with degenerative activity, in rat brain

The calcium-activated protease calpain I was localized in rat brain by immunocytochemistry. Calpain I-like immunoreactivity (CLI) was prominent in several structures in which degeneration is an ongoing feature, e.g. spinal motoneurons, olfactory nerve. Also noteworthy was the presence of CLI in regions susceptible to age-related pathologies, e.g. cerebellar Purkinje cells, substantia nigra and subiculum. This distribution suggests that calpain I may be involved with both normal and pathological neuronal degeneration.