Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P50502 (Hip)
7,003 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Leptin concentrations in humans are increased with obesity, and women have higher leptin concentrations than men. This sex difference reflects the greater fat mass of women. However, there is evidence that factors other than the size of the adipose tissue mass contribute to serum leptin concentrations. This study was undertaken to determine whether anthropometric factors influenced leptin concentrations in our population. Leptin concentrations were measured in 375 persons from a population study of hypertension and diabetes for whom body-composition data (bio-electrical impedance analysis and anthropometry) were available. Serum leptin concentrations were more than four times higher in women than in men (18.5 +/- 13.9 compared with 3.8 +/- 3.6 ng/L, P < 0.0001). In individuals with comparable body mass indexes, these differences persisted after adjustment for either percentage fat (P < 0.05) or fat mass (P < 0.0001) by multivariate-regression analysis. After fat mass was adjusted for, the serum leptin concentration in both men and women was independent of waist circumference but in women was associated with hip circumference. Hip circumference is a proxy measure of peripheral fat and these results suggest that the larger hips of women may contribute to the sex difference in serum leptin concentration.
Am J Clin Nutr 1997 Dec
PMID:Leptin concentration in women is influenced by regional distribution of adipose tissue. 973 58

Inhibition of angiotensin converting enzyme(ACE) in presence of captopril(C), lisinopril(L) and enalapril(E) were investigated in testis and epididymis of sheep using Hip-His-Leu as substrate. Captopril, lisinopril and enalapril were competitive inhibitors of the enzyme from both tissues. Differences in the I50 and Ki values using these three inhibitors reflects the affinities of these inhibitors for the ACE. In addition, the relative potencies of captopril, lisinopril and enalapril were different for testicular ACE(C > L > E) and epididymal ACE(L > C > E). This observation suggests differences between the active sites of the testicular and epididymal ACE which may reflect on their functions in vivo.
Biochem Mol Biol Int 1997 Dec
PMID:Sheep testicular and epididymal angiotensin converting enzyme: inhibitions by captopril, lisinopril and enalapril. 941 15

As a result of the improvement in the resolution of diagnostic sonography equipment it is possible to depict sonographic echoes of structures in the area of the preformed cartilage acetabular roof, especially in the region of the proximal perichondrium, perichondrial gap and the joint capsule that up to now have not been anatomically identified. Therefore, the question arises as to which anatomical structures these newly observed sonographic echoes can be classed with. Hip-joint NMR images of corpses were made and compared to anatomical specimen, anatomical sections and sonograms of high-resolution ultrasound equipment. Through this comparative study it was possible to demonstrate that the echo of the proximal perichondrium is anatomically consistent with the proximal perichondrium itself, parts of the joint capsule and the insertion of the musculus rectus femoris tendon. Identification of the ligamentum ischiofemorale and its separation from the labrum acetabulare, the joint capsule and the musculus rectus femoris tendon leads to better interpretation of the perichondrial gap in the sonogram. Common terms, such as "proximal perichondrium" and "perichondrial gap" obtain a new anatomical assessment. These terms, taken as a basis for knowledge of the anatomical structures, can be used as usual. There are no consequences for hip sonography today if the definition of the distinction between type III and type IV, and of the standard section is used further as the basis of sonography even if these terms have received a new anatomical classification.
Orthopade 1997 Dec
PMID:[Redefinition of the proximal perichondrium and perichondrial gap in hip ultrasound imaging]. 949 10

Hip-Arg-Phe-, Hip-Phe-Arg- and Hip-His-Leu-cleaving dipeptidyl carboxypeptidase activities were measured in the supernatant (S2) and pellet (P2) fractions obtained by ultracentrifugation of human adrenal tumor preparations. Negligible enzyme activity was found in cortical tumor whereas highly significant activities were present in the P2 fractions of the two pheochromocytoma specimens. The hydrolysis rates, expressed in terms of the percent of added substrate were 58-66%/60 min for Hip-Phe-Arg, 55-58%/60 min for Hip-Arg-Phe and 19-30%/60 min for Hip-His-Leu. The angiotensin-converting enzyme inhibitor, captopril, differentially inhibited the enzyme splitting Hip-His-Leu versus the one cleaving Hip-Arg-Phe; Hip-Phe-Arg is probably the substrate of both. It is concluded that the Hip-Arg-Phe-cleaving enzyme in adrenomedullary tumor is probably identical to the purportedly novel dipeptidyl carboxypeptidase that we detected earlier in rabbit ear artery wall, which converts (Met5)-enkephalin-Arg6,Phe7 to (Met5)-enkephalin.
Neuropeptides 1997 Dec
PMID:Hip-Arg-Phe-, Hip-Phe-Arg- and Hip-His-Leu-cleaving dipeptidyl carboxypeptidases in human adrenal tumors. 957 25

Inhibition of angiotensin converting enzyme(EC 3.4,15.1, ACE) in presence of captopril, lisinopril and enalapril were investigated in kidney, lung and serum of sheep using Hip-His-Leu(HHL) as substrate. The activity in kidney, lung and serum was inhibited at HHL concentration above 5 mM. The inhibitory constants (IC50) ranged between 5.6 nM for serum ACE with lisinopril and 70000 nM for renal ACE with enalapril while Ki ranged from 1.0 nM for serum ACE with lisinopril to 12000 nM for kidney ACE with enalapril. Differences in inhibition observed in different tissues suggest that the inhibitors may block function(s) of ACE to varying degrees in each tissue.
Indian J Biochem Biophys 1997 Dec
PMID:Inhibition of angiotensin converting enzyme from sheep tissues by captopril, lisinopril and enalapril. 959 34

Retrieval studies suggest that the loosening process of the cemented femoral components of total hip arthroplasties is initiated by failure of the bond between the prosthesis and the cement mantle. Finite element (FE) analyses have demonstrated that stem-cement debonding has stress-producing effects in the cement mantle. High interface friction, which corresponds to a degree of surface roughness, reduces these stresses. In experiments, however, debonded rough stems produced more cement damage than polished ones; in the Swedish Hip Register polished stems were clinically superior with respect to stems with a mat surface finish. The purpose of the present study was to investigate this contradiction. For this purpose, global and local FE models with debonded stem-cement interfaces were used to study the effects of prosthesis surface roughness on the cement stresses on a global scale and microscale, respectively. Similar to earlier numerical studies, the global FE model predicted that an increased surface roughness of the stem reduced the stresses in the cement mantle. The local model provided insight in the load-transfer mechanism on a microscale and could explain the experimental and clinical findings. The local cement peak stresses around the asperities of the surface roughness profile increased with increasing surface roughness and decreased again beyond a particular roughness value. Cement abrasion is caused by localized stresses in combination with micromotion. From this study it can be concluded that to minimize cement abrasion, debonded stems should either have a polished microstructure to minimize the local cement stresses or have a profiled macrostructure to minimize micromotions at the stem-cement interface.
J Biomed Mater Res 1998 Dec 15
PMID:Effects of prosthesis surface roughness on the failure process of cemented hip implants after stem-cement debonding. 982 79

The progesterone receptor can be reconstituted into hsp90-containing complexes in vitro, and the resulting complexes are needed to maintain hormone binding activity. This process requires ATP/Mg2+, K+, and several axillary proteins. We have developed a defined system for the assembly of progesterone receptor complexes using purified proteins. Five proteins are needed to form complexes that are capable of maintaining hormone binding activity. These include hsp70 and its co-chaperone, hsp40, the hsp70/hsp90-binding protein, Hop, hsp90, and the hsp90-binding protein, p23. The proteins Hip and FKBP52 were not required for this in vitro process even though they have been observed in receptor complexes. Each of the five proteins showed a characteristic concentration dependence. Similar concentrations of hsp70, hsp90, and p23 were needed for optimal assembly, but hsp40 and Hop were effective at about 1/10 the concentration of the other proteins, suggesting that these two proteins act catalytically or are needed at levels similar to the receptor concentration. ATP was required for the functioning of both hsp70 and hsp90. The binding of hsp70 to the receptor requires hsp40 and about 10 microM ATP; however, hsp90 binding appears to occur subsequent to hsp70 binding and is optimal with 1 mM ATP. A three-step model is presented to describe the assembly process.
J Biol Chem 1998 Dec 04
PMID:The assembly of progesterone receptor-hsp90 complexes using purified proteins. 983 49

We evaluated different definitions of osteoporosis in a population-based sample of 348 men (age 22-90 years) compared with 351 women (age 21-93 years). Thirty-six men (10%) and 46 women (13%) had a history of osteoporotic fracture (hip, spine, or distal forearm due to moderate trauma at >/= age 35). In logistic regression analysis, osteoporotic fracture risk was associated with bone mineral density (BMD) at all sites (neck, trochanter, total hip, lumbar spine, and total wrist) in both genders (p < 0.001) except spinal BMD in men. After adjusting for age, total hip BMD was the strongest predictor of fracture risk in women (odds ratio [OR] per 1 SD decline, 2.4; 95% confidence interval [CI], 1.6-3.7), while wrist BMD was best in men (OR, 1.5; 95% CI, 1.1-2.0). Among men but not women, bone mineral apparent density (BMAD) was a better predictor of fracture than BMD (wrist BMAD OR, 1.7; 95% CI, 1.3-2.3). Hip BMD/BMAD decreased linearly from age 20 years onward in both genders, while spinal BMD/BMAD declined after age 40 in women but not in men. In both genders, total wrist BMD/BMAD decreased after age 50. By World Health Organization criteria, the age-adjusted prevalence of osteoporosis at the hip, spine, or wrist was 35% among women >/=50 years of age. A similar approach (BMD > 2.5 SD below the young male mean) produced an osteoporosis prevalence rate in men >/=50 years of age of 19%. Thus, bone density predicts fracture risk in men as it does in women, and the prevalence of osteoporosis in men, using sex-specific normal values, is substantial. These observations indicate a need for better prevention and treatment strategies for men.
J Bone Miner Res 1998 Dec
PMID:Bone density and fracture risk in men. 984 10

Hip fractures are recognized as a major public health problem worldwide. Demographic changes will lead to enormous increases in the number of hip fractures and projections indicate that the number of hip fractures occurring worldwide each year will rise from 1.26 million in 1990 to 4.5 million by 2050. However, preventive strategies are available. Supplementation with Ca2+ and vitamin D restores bone quality through suppression of secondary hyperparathyroidism and decreases the risk of falling through improvement of neuromuscular coordination and body sway. This leads to a reduction of hip fracture risk of 43% in the vitamin D-insufficient elderly. Treatment with the bisphosphonate alendronate increases bone strength and results in a 51% reduction of hip fracture risk. Hip protectors absorb energy during a fall and reduce hip fracture risk by 56%. Combining these three procedures could prevent a large proportion of hip fractures in the future.
Trends Endocrinol Metab 1999 Dec
PMID:Vitamin D and Hip Fracture. 1054

Rapid and transient activation of heat shock genes in response to stress is mediated in eukaryotes by the heat shock transcription factor HSF1. It is well established that cells maintain a dynamic equilibrium between inactive HSF1 monomers and transcriptionally active trimers, but little is known about the mechanism linking HSF1 to reception of various stress stimuli or the factors controlling oligomerization. Recent reports have revealed that HSP90 regulates key steps in the HSF1 activation-deactivation process. Here, we tested the hypothesis that components of the HSP90 chaperone machine, known to function in the folding and maturation of steroid receptors, might also participate in HSF1 regulation. Mobility supershift assays using antibodies against chaperone components demonstrate that active HSF1 trimers exist in a heterocomplex with HSP90, p23, and FKBP52. Functional in vivo experiments in Xenopus oocytes indicate that components of the HSF1 heterocomplex, as well as other components of the HSP90 cochaperone machine, are involved in regulating oligomeric transitions. Elevation of the cellular levels of cochaperones affected the time of HSF1 deactivation during recovery: attenuation was delayed by immunophilins, and accelerated by HSP90, Hsp/c70, Hip, or Hop. In immunotargeting experiments with microinjected antibodies, disruption of HSP90, Hip, Hop, p23, FKBP51, and FKBP52 delayed attenuation. In addition, HSF1 was activated under nonstress conditions after immunotargeting of HSP90 and p23, evidence that these proteins remain associated with HSF1 monomers and function in their repression in vivo. The remarkable similarity of HSF1 complex chaperones identified here (HSP90, p23, and FKBP52) and components in mature steroid receptor complexes suggests that HSF1 oligomerization is regulated by a foldosome-type mechanism similar to steroid receptor pathways. The current evidence leads us to propose a model in which HSF1, HSP90 and p23 comprise a core heterocomplex required for rapid conformational switching through interaction with a dynamic series of HSP90 subcomplexes.
Mol Cell Biol 1999 Dec
PMID:Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 In vivo. 1056 29


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