𝔖 Bobbio Scriptorium
✦   LIBER   ✦

EXPRESSION AND CELLULAR LOCALIZATION OF THE mRNA FOR THE 25-kDa HEAT-SHOCK PROTEIN IN THE MOUSE

✍ Scribed by TOMOHIKO WAKAYAMA; SHOICHI ISEKI


Publisher
Elsevier Science
Year
1998
Tongue
English
Weight
403 KB
Volume
22
Category
Article
ISSN
1065-6995

No coin nor oath required. For personal study only.

✦ Synopsis


The 25-kDa heat-shock protein (Hsp25) is a member of the small heat-shock protein family but its function remains largely unknown. In the present study we examined the expression and cellular localization of Hsp25 mRNA in mice under physiological, unstressed conditions using Northern blot and in situ hybridization analyses with specific oligonucleotide probes. At the organ level, high amounts of Hsp25 mRNA were detected in the oesophagus, skin,eye, stomach, lung and urinary bladder, with moderate amounts in the heart, skeletal muscle, aorta, adrenal gland, ovary, testis, uterus, large intestine, and thymus. At the cellular level, intense to moderate signals for Hsp25 mRNA were localized in the muscle cells of smooth, heart and skeletal types, in the epithelial cells of stratified squamous and transitional types and of the oviduct, in the steroid endocrine cells of the adrenal cortex and corpus luteum, as well as in the spermatocytes of the testis. In contrast, the signal was scarcely detectable in the nervous tissues, lymphatic tissues, the columnar epithelial cells of the digestive tract, or the parenchymal cells of the liver, pancreas and kidney. These results suggest some significant role for Hsp25 in distinct populations of mouse cells under physiological conditions.


πŸ“œ SIMILAR VOLUMES


Constitutive expression of the 25-kDa he
✍ Armstrong, Carol L.; Krueger-Naug, Anne Marie; Currie, R. William; Hawkes, Richa πŸ“‚ Article πŸ“… 2000 πŸ› John Wiley and Sons 🌐 English βš– 838 KB

Despite the reported absence of the 25-kDa heat shock protein Hsp25 in the rodent cerebellum, we have determined that Hsp25 is constitutively expressed in a subset of Purkinje cells in the adult cerebellum of the mouse. No other cerebellar neurons are Hsp25 immunoreactive, but there is weak staining

CELL SURFACE LOCALIZATION OF THE 60 kDa
✍ BOHDAN J. SOLTYS; RADHEY S. GUPTA πŸ“‚ Article πŸ“… 1997 πŸ› Elsevier Science 🌐 English βš– 158 KB

## Abstract To investigate whether the 60‐kDa heat shock chaperonin protein (hsp60) is present on the surface of mammalian cells, we used immunogold labeling of intact cells and backscattered electron imaging to image gold particles. Chinese hamster ovary cells and the human leukemic CD4‐positive T

Expression of heat shock and cold shock
✍ Kingsley, Roni J. ;Afif, Evelyn ;Cox, Brandon C. ;Kothari, Sonali ;Kriechbaum, K πŸ“‚ Article πŸ“… 2003 πŸ› John Wiley and Sons 🌐 English βš– 195 KB πŸ‘ 1 views

In this study, we analyzed the response of the temperate, shallow-water gorgonian, Leptogorgia virgulata, to temperature stress. Proteins were pulse labeled with (35)S-methionine/cysteine for 1 h to 2 h at 22 degrees C (control), or 38 degrees C, or for 4 h at 12.5 degrees C. Heat shock induced synt

Hypoglycemia enhances the expression of
✍ W.-C. Shyu; C.-P. Chen; K. Saeki; A. Kubosaki; Y. Matusmoto; T. Onodera; D.-C. D πŸ“‚ Article πŸ“… 2005 πŸ› John Wiley and Sons 🌐 English βš– 384 KB πŸ‘ 2 views

Cellular prion protein (PrP(C)) expression can be regulated by heat-shock stress, and we designed the present study to determine whether hypoglycemia could affect PrP(C) expression. RT-PCR and Western blotting were used to measure the expression of PrP(C) and heat-shock protein (Hsp70) in mouse neur