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lens/phosphatase
Линкът е запазен в клипборда
Страница 1 от 160 резултата
Osteogenic differentiation of human lens epithelial cells might contribute to lens calcification.
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Calcification of the human lens has been described in senile cataracts and in young patients with congenital cataract or chronic uveitis. Lens calcification is also a major complication of cataract surgery and plays a role in the opacification of intraocular lenses. A cell-mediated process has been
18 kDa protein tyrosine phosphatase in the ocular lens.
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Protein tyrosyl phosphorylation and dephosphorylation play essential roles in regulating cellular events such as proliferation and differentiation, and their involvement in the lens development and transparency is also suggested. The level of tyrosine phosphorylation in a given protein is regulated
[Phosphatase activity in various zones of bovine crystalline lens].
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Acid phosphatase and lipid peroxidation in human cataractous lens epithelium.
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The anterior lens epithelial cells undergo a variety of degenerative and proliferative changes during cataract formation. Acid phosphatase is primarily responsible for tissue regeneration and tissue repair. The lipid hydroperoxides that are obtained by lipid peroxidation of polysaturated or
Acid phosphatase in lens epithelium of rabbits after x-irradiation.
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Phosphorylation of HSP25 during lens cell differentiation.
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Small heat shock proteins and alpha-crystallins are related proteins with several common structural and functional properties including homologous amino acid sequences and similar chaperone-like activity. Furthermore, small heat shock proteins and alpha-crystallins are phosphorylated in vivo at
Acid hydrolases in the bovine lens epithelium.
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Acid hydrolases (acid phophatase, N-acetyl-beta-D-glucosaminidase, alpha-D-mannosidase, alpha-L-fucosidase, and beta-D-glucuronidase) in the bovine lens epithelium were studied biochemically. p-Nitrophenyl derivatives were used as substrate. All enzymatic activity was found to be much higher in the
Purinergic receptor-mediated regulation of lens connexin43.
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OBJECTIVE
To determine whether the purinergic receptor-mediated, delayed transient inhibition of lens cell-to-cell communication is due to the protein kinase C (PKC)-catalyzed phosphorylation of connexin (Cx)43.
METHODS
The functional activity of gap junctions was determined in the presence of
A high phosphotyrosine phosphatase activity is present in differentiating bovine lens cells.
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Activity of phosphotyrosine-protein phosphatases (PTPases) has been investigated in the different cellular regions of bovine eye lens. PTPases were tested in cellular detergent extracts using phospholabelled synthetic peptides and p-nitrophenyl phosphate. We show that a high PTPase activity is only
Retroviral expression of connexins in embryonic chick lens.
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OBJECTIVE
To develop an in vivo model system in which exogenous proteins can be expressed in embryonic chick lens and to further understand the function of connexin-mediated gap junction intercellular communication in lens cell biology.
METHODS
RCAS(A) is a replication-competent chicken retrovirus
The dephosphorylation of lens alpha-crystallin A chain.
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The present communication reports the presence of a phosphoprotein phosphatase activity in bovine lens preparations which dephosphorylates alpha Ap, the phosphorylated form of alpha A, one of the alpha-crystallin polypeptides, in a Ca2+/calmodulin dependent manner. The activity was found in soluble
DNase IIbeta distribution and activity in the mouse lens.
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OBJECTIVE
To map the cellular and subcellular distribution of DNase IIbeta activity in the mouse lens.
METHODS
DNase IIbeta-specific activity was determined by assaying lens lysates prepared from wild-type or DNase IIbeta-null mice. Regional nuclease activity was determined by microdissection of
Posttranslational phosphorylation of lens fiber connexin46: a slow occurrence.
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OBJECTIVE
To study in both in situ and primary cultures the posttranslational phosphorylation of connexin46 (Cx46), one of two members of the connexin family of gap junction proteins expressed by lens fibers.
METHODS
Phosphatase digestion, gel electrophoresis, cell culture, organ culture,
Predominant phosphatase in the ocular lens regulated by physiological concentrations of magnesium and calcium.
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A magnesium-dependent phosphatase with a molecular weight of about 55 kDa was found in the lens of chicken embryo, mouse, rabbit and bovine. It appears to be unique to the lens and, when activated by magnesium, accounts for the majority of the phosphatase activity in the lens. Phosphatases in the
Activation of phosphotyrosine phosphatase activity is associated with decreased differentiation in adult bovine lens.
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The postnatal vertebrate eye lens provides an opportunity to study possible involvement of reversible protein phosphorylation in the differentiation process of epithelial cells. Epithelial cells at the lens equator, indeed, differentiate continuously into fiber cells throughout life but this
Най-пълната база данни за лечебни билки, подкрепена от науката
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