Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.10.2 (focal adhesion kinase)
 44,029 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have analyzed the protein content of proximal tubular fluid (PTF) by ultramicro disc electrophoresis and measured total protein excretion rates both in control conditions and during angiotensin infusion to the rat. Under control conditions PTF albumin concentration was 1.49 +/- 1.12 (SD) mg/100 ml and did not increase with distance from the glomerulus. Immediate postcapsular samples (Munich-Wistar strain) yielded nearly identical values so that both probably represent filtered albumin concentration. During infusion of angiotensin (0.15 mug/mix x 100 g of body wt), PTF albumin concentration increased on the average 26-fold in re-collections from control tubules. Total protein excretion increased from a control of 7.91 to 24.37 mg/24 hr x 100 g of body wt. Glomerular filtration rate (FGR), single nephron GFR (SNGFR), proximal transit time and tubular fluid to plasma (tf/p) inulin values did not change significantly. Net afferent filtration pressure decreased from 24.7 to 15.6 mm Hg and renal plasma flow fell from 2.16 to 1.31 mo/min x g of kidney wt. Data describe a protein reabsorptive system normally operating near capacity. Angiotensin-induced proteinuria derives from an increase in filtered protein (mostly albumin) resulting from permeability changes in the glomerular membrane.
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PMID:Effect of angiotensin on the filtration of protein in the rat kidney: a micropuncture study. 116 Feb 30

The effects of uremia-induced chronic acidosis on fractional protein synthesis rate (FSR), degradation (FDR) and protein tissue growth (FRG) in skeletal muscle were examined in young rats fed a 30% protein diet. This diet induced acidosis in UA rats, which was corrected by NaHCO3 supplementation in UB rats. Blood pH and plasma HCO3- were 7.22 +/- 0.01 and 15.2 +/- 0.8 mmol/l in UA rats vs. 7.41 +/- 0.01 and 25.8 +/- 0.9 in UB rats. Both UA and UB groups had similar renal function and food intake. Acidosis impaired weight gain (4.0 +/- 0.3 vs. 5.0 +/- 0.4 g/day, p < 0.05) and length gain (0.31 +/- 0.02 vs. 0.42 +/- 0.02 cm/day, p < 0.001). UA and UB rats showed similar muscle FSR (10.4 +/- 0.5 vs. 10.8 +/- 0.5%/day) and RNA content (6.3 +/- 0.2 vs. 6.2 +/- 0.2 micrograms/g protein). UA rats had lower FGR than UB rats (3.9 +/- 0.8 vs. 5.9 +/- 0.6%/day, p < 0.05). Therefore, muscle FDR was increased in UA rats (6.30 +/- 0.99 vs. 5.10 +/- 0.7%/day).
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PMID:Protein synthesis and growth in uremic rats with and without chronic metabolic acidosis. 146 69

IL-2 is one of the principal growth factors regulating the proliferation of T lymphocytes. Although two independent IL-2-binding molecules have been molecularly cloned and shown to participate in the formation of a high affinity receptor complex, their primary structures do not suggest a specific mechanism for IL-2 growth signal transduction across the cell membrane. Neither IL-2 receptor subunit contains an intrinsic kinase domain; nevertheless, tyrosine phosphorylation of various intracellular substrates is one of the first biochemical changes observed following activation of the IL-2 receptor (IL-2R). Both serine/threonine and tyrosine kinases can be co-precipitated as part of the IL-2R complex suggesting that the IL-2 signalling may involve the activation of non-covalently associated intracellular kinases. However, controversy exists as to which kinases are involved in IL-2 signal transduction; in particular, which kinase(s) mediates the first or proximal event(s) in the signalling process. Activation of the IL-2R leads to serine and threonine phosphorylation of the SRC tyrosine kinase family member, LCK, and an increase in LCK tyrosine kinase activity. Furthermore, LCK can be co-immunoprecipitated with the beta chain of the IL-2R indicating its association with the receptor complex. IL-2 has also been reported to increase FYN kinase activity and to alter its association with the 85 kDa subunit of phosphatidylinositol-3 kinase thus suggesting a role for FYN in IL-2 signal transduction. However, in this report, we now demonstrate that neither LCK nor FYN are obligatory for IL-2-induced growth of HTLV-I-infected human T cells. Lack of expression of LCK or FYN in the HTLV-I-infected T cell lines was demonstrated by a combination of Northern blotting, polymerase chain reaction, Western blotting, and in vitro kinase activity. Despite the absence of LCK or FYN, IL-2 induced similar patterns of rapid tyrosine phosphorylation. Similar results were observed in cell lines lacking expression of the LYN, FGR, HCK, and LTK tyrosine kinases. Thus, none of these tyrosine kinases alone appears to be required for growth signalling through the IL-2R in the HTLV-I-infected T cell lines analyzed. The findings raise the possibility that an, as yet, unidentified tyrosine kinase is involved. Alternatively, this biological signalling system may exhibit remarkable redundancy whereby several different tyrosine kinases may be capable of associating with the IL-2R complex and mediating intracellular signalling.
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PMID:Neither the LCK nor the FYN kinases are obligatory for IL-2-mediated signal transduction in HTLV-I-infected human T cells. 147 76

The expression of protein-tyrosine kinases (PTKs; ATP:protein-tyrosine O-phosphotransferase, EC 2.7.1.112) was studied in normal human lung and various tumors by PCR followed by molecular cloning and sequence analysis. Six known PTKs (YES, FGR, LYN, HCK, PDGFB-R, and CSF1-R), as well as two additional members of this enzyme family, were detected in lung. One of the newly discovered sequences appears to represent a group of cytosolic PTKs. The cDNA sequence of the second unknown PTK revealed that it is a fourth member of the fibroblast growth factor receptor family. It was therefore called TKF (tyrosine kinase related to fibroblast growth factor receptor). Among a wide variety of cells and tissues tested, including human lymphocytes and macrophages, TKF was only found expressed in lung. Apart from normal lung, TKF expression could be demonstrated in some tumors of lung origin, but also in malignancies not derived from lung tissues. As fibroblast growth factors are generally involved in a variety of functions such as mitogenesis, angiogenesis, and wound healing, the specific expression of a receptor-related gene in lung only may point to yet another special function of this group of proteins.
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PMID:Two additional protein-tyrosine kinases expressed in human lung: fourth member of the fibroblast growth factor receptor family and an intracellular protein-tyrosine kinase. 172 May 39

The article deals with the comparative evaluation of the immobilizing properties of the "boot" plaster bandage after manual and apparatus reposition of the malleoli. It was revealed by means of the EMED and F P/10 apparatus (FGR) that the immobilizing property of the "boot" plaster bandage is higher in apparatus than in manual reposition.
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PMID:[A comparative study of immobilizing properties of the "boot" plaster bandage after manual and device reposition of fractures of the malleolus]. 175 38

Recent studies of the FGR protooncogene have shown that expression of its mRNA is limited to mature peripheral blood granulocytes, monocytes, and tissue macrophages. In the present study, we have investigated p55c-fgr expression in normal human neutrophils [polymorphonuclear leukocytes (PMN)] and have found enzymatically active p55c-fgr to be abundant in lysates of PMN and murine fibroblasts transfected with a FGR expression plasmid but not control cells. Fractionation studies revealed that neutrophil p55c-fgr was present in plasma membrane-enriched fractions as well as fractions containing secondary and tertiary granules. Little change in the distribution of p55c-fgr or FGR kinase activity was observed under conditions favoring tertiary granule release. In contrast, when secondary granule secretion was induced with the chemoattractant peptide, formyl-Met-Leu-Phe, a marked decrease in p55c-fgr and FGR kinase was observed in fractions depleted of secondary granules. Concomitantly, the relative concentration of p55c-fgr and its enzymatic activity were increased in fractions containing plasma membrane. From these findings we conclude that p55c-fgr is associated with functional secretory granules and is redistributed within normal neutrophils in response to their activation.
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PMID:Translocation of the FGR protein-tyrosine kinase as a consequence of neutrophil activation. 268 59

A restriction fragment length polymorphism (RFLP) at the human FGR gene, a member of the src family of protooncogenes, has been identified and used to locate FGR on the genetic linkage map of human chromosome 1p. Single-copy sequences subcloned from a cosmid containing the human FGR gene were used to screen a panel of genomic DNAs for RFLPs. One plasmid, designated pB8, detected a high-frequency EcoRI RFLP (allele frequencies, 0.57/0.43). Analysis of a panel of somatic cell hybrids demonstrated that pB8 maps to the region 1p31-pter. Genetic linkage analysis of the 40 families provided by the Centre d'Etude du Polymorphisme Humain (CEPH) showed that FGR maps to a location 3.1 cM from the Rh blood group locus (RH), and falls in the 17.5-cM gap between alpha-fucosidase (FUCA1) and D1S57. The relative gene order of RH and FGR could not be determined unequivocally, but the most favored gene order was 1pter-PND-ALPL-FUCA1-FGR-RH-D1S57-MYCL.
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PMID:Localization of the FGR protooncogene on the genetic linkage map of human chromosome 1p. 290 22

This study concerns 152 neonates admitted between June 1981 and December 1983 in a neonatal intensive care unit. It aims to evaluate brain growth and to analyse the influence of intrauterine growth retardation (IUGR), intracranial haemorrhage (ICH) and ventricular dilatation (VD) in pre-term infants. The babies were first analysed at birth. The sample comprised 127 normal infants and 25 IUGR neonates. An ultrasonic index of cerebral growth was devised: the height of the frontal lobes (HFL), measured in a standardised coronal slice of the brain. According to gestational age (GA), HFL and head circumference (HC) gave a similar assessment of brain growth. A regression line of normal intrauterine values of HFL has been produced according to GA and might be added to the other ways of following the intrauterine growth of the brain after 26 weeks. Brain growth was slower in IUGR, when assessed both by HFL and HC. The infants were also assessed during the postnatal period for a mean period of 27.6 days (S.E.M.: 3.5). They were divided into 5 groups: 45 preterm infants without IUGR, ICH or VD; 45 preterm neonates with ICH alone; 12 preterm babies with ICH and VD alone, 10 preterm infants with isolated FGR, and 8 preterm neonates with IUGR and ICH. A calculation of the global anthropometric (body weight, body length, HC and HFL) weekly increment was made for all infants according to their respective group. No statistical difference in any of these parameters between these 5 groups emerged.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Brain growth in sick newborn infants: a clinical and real-time ultrasound analysis. 351 1

A growth regulatory factor, which reversibly inhibits DNA synthesis and proliferation of fibroblasts, has been isolated from medium conditioned by exposure to density-inhibited mouse 3T3 cells. This factor, termed FGR-s (13K), yielded a single polypeptide (Mr 13,000) when analyzed by SDS PAGE under both reducing and nonreducing conditions. The dose-response curve of growth inhibition by FGR-s (13K) showed that 50% inhibition of 3T3 cell proliferation was achieved at a concentration of approximately 3 ng/ml, corresponding to approximately 0.23 nM. The activity of FGR-s (13K) was depleted by passing the material over an affinity column containing the monoclonal antibody 2A4; this monoclonal antibody had been previously characterized to bind to the Mr 13,000 polypeptide. These results indicate that we have purified a growth regulatory factor that acts to inhibit the proliferation of cells in an autocrine pathway.
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PMID:Growth control in cultured 3T3 fibroblasts. V. Purification of an Mr 13,000 polypeptide responsible for growth inhibitory activity. 394 88

Fractional rates (% X day-1) of synthesis and degradation were determined by measuring the output of N tau-methylhistidine (MeHis) in the excreta at 4 and 8 weeks of age in the chicken. At 4 weeks of age, the fractional rate of synthesis of the meat-type stock was twice that of the egg-type stock (White Leghorn), but the fractional rates of synthesis at 8 weeks of age were similar (4.1-5.1% X day-1) among stocks. The fractional rate of degradation (1.3-1.5% X day-1) of the meat-type stock at 8 weeks of age was less than half the rate of the egg-type stock (2.9% X day-1). The fractional rates of synthesis and degradation at 4 weeks of age in the Satsuma native fowl were relatively high compared with those in the other stocks. In particular, the rate of degradation (8.6% X day-1) at 4 weeks of age was approximately twice that of other stocks. These results show that fractional rates of synthesis and degradation of muscle protein in the chicken differ among genetically diverse groups. The effect of changes in rates of synthesis and degradation on the change in fractional growth rate also differed. From regression coefficients (bks . FGR and bKd . FGR) of these rates in skeletal muscle protein on the fractional growth rate, it was recognized that the change in growth rate accompanies the changes in both synthesis and degradation in White Leghorn and commercial broilers but only the change in synthesis in White Plymouth Rock (dw) and Satsuma native fowl.
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PMID:Variation among chicken stocks in the fractional rates of muscle protein synthesis and degradation. 649 31


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