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sida/phosphatase

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Monoclonal antibodies against placental-like and intestinal-like alkaline phosphatases in a malignant human cell line.

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Monoclonal antibodies were raised against alkaline phosphatase (ALP) from the malignant human cell line Hep2, a derivative of HeLa, which was established from a cervical carcinoma. Two forms of ALP are found in Hep2 cells resembling, but not identical to, the normal placental and intestinal ALPs.

Placental-like alkaline phosphatase in seminoma.

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Tumor marker identification in testicular cancer has contributed to early detection and monitoring of non-seminomatous disease. A placental alkaline phosphatase-like (PLAP-like) enzyme derived from seminomas has recently been focused upon as a possible marker for this disease. The biochemistry of

Structure and expression of phosphoglucan phosphatase genes of Like Sex Four1 and Like Sex Four2 in barley.

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Phosphoglucan phosphatases (Like-SEX4 1 and 2; LSF1 and LSF2) were reported to play roles in starch metabolism in leaves of Arabidopsis. In this study, we identified and mapped the LSF1 and LSF2 genes in barley (HvLSF1 and HvLSF2), characterized their gene and protein structures, predicted the

The immunoglobulin-like domains 1 and 2 of the protein tyrosine phosphatase LAR adopt an unusual horseshoe-like conformation.

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Neurogenesis depends on exquisitely regulated interactions between macromolecules on the cell surface and in the extracellular matrix. In particular, interactions between proteoglycans and members of the type IIa subgroup of receptor protein tyrosine phosphatases underlie crucial developmental

Placenta-like alkaline phosphatase in gynecological cancers.

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In 302 patients with tumors of the cervix, corpus uteri, and ovaries, assessment by clinical staging (tumors-nodules-metastasis system) (4) and histopathology has been related to the presence of serum heat-stable, placenta-lide alkaline phosphatase (PLAP) activity. Early stages of cervical tumors

Characterization of seminoma-derived placental-like alkaline phosphatase.

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Characteristics of placental-like alkaline phosphatase (PLAP-like enzyme) in seminoma was studied. By use of lectin affinity chromatography, PLAP-like enzyme in seminoma revealed extra sugar chains compared to placental alkaline phosphatase (PLAP), indicating heterogeneity of the carbohydrate

Placenta-like alkaline phosphatases from human osteosarcoma cells.

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Hormone-induced alkaline phosphatases in human osteosarcoma cells (LM) were extracted and purified. Characterization of the purified enzyme showed two distinct isoenzymes. One isoenzyme was heat labile, was homoarginine inhibited, and had the electrophoretic migration of alkaline phosphatase of

The "VH1-like" dual-specificity protein tyrosine phosphatases.

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The number of dual-specificity protein tyrosine phosphatases has grown considerably in the last few years, and thus it would be helpful to organize these novel enzymes. The simple term "VH1-like" or "dual-specificity" phosphatase does not adequately reflect the different subclasses within this new

Transmembrane homodimerization of receptor-like protein tyrosine phosphatases.

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Receptor-like protein tyrosine phosphatases (RPTPs) are type I integral membrane proteins. Together with protein tyrosine kinases, RPTPs regulate the phosphotyrosine levels in the cell. Studies of two RPTPs, CD45 and PTPalpha, have provided strong evidence that dimerization leads to inactivation of

A unique bone-like variant of alkaline phosphatase.

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The authors describe an unusual variant of alkaline phosphatase (ALP) discovered in a patient with a 90-fold increase in serum ALP. The variant ALP was indistinguishable from the bone isoenzyme when subjected to chemical inhibition, heat inactivation, lectin precipitation, and routine

Protein tyrosine phosphatase-like proteins: link with IDDM.

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It has been shown that insulin-like growth factor-I (IGF-I) stimulates the activity of alkaline phosphatase, a marker of mature osteoblast phenotype, in osteoblasts. In the present study, we investigated the involvement of the mitogen-activated protein (MAP) kinase superfamily in the

Placenta-like isoenzyme of alkaline phosphatase in prostatic cancer.

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Assays for serum placenta-like (Regan) isoenzyme of alkaline phosphatase were done on 157 samples from 96 patients with prostatic cancer entered into various National Prostatic Cancer Project protocols. Elevated placenta-like isoenzyme levels were found in 19 patients (20 per cent). Increased

Protein Ser/Thr phosphatases with kelch-like repeat domains.

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This report describes the presence in plants of protein Ser/Thr phosphatases of the PPP family, homologous to PfPPalpha phosphatase from Plasmodium falciparum. Like PfPPalpha, they possess large N-terminal domains and catalytic domains that are more closely related to the protein phosphatase 1

Widespread presence of "bacterial-like" PPP phosphatases in eukaryotes.

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BACKGROUND In eukaryotes, PPP (protein phosphatase P) family is one of the two known protein phosphatase families specific for Ser and Thr. The role of PPP phosphatases in multiple signaling pathways in eukaryotic cell has been extensively studied. Unlike eukaryotic PPP phosphatases, bacterial
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