NDLI: Ultrastructural localization of Hsp-72 examined with a new polyclonal antibody raised against the truncated variable domain of the heat shock protein

Please wait, while we are loading the content...

Ultrastructural localization of Hsp-72 examined with a new polyclonal antibody raised against the truncated variable domain of the heat shock protein

Content Provider	PubMed Central
Author	Kurucz, Istrán Tombor, Bálint Prechl, József Erdö, Franciska Hegedüs, Erzsébet Nagy, Zoltán Marta, Vitai Korányi, Lászlo Lajos, Lászlo
Copyright Year	1999
Abstract	In spite of the intensive search for the determination of the continuously widening physiological and pathological roles of different stress proteins, their ultrastructural localization at the electron microscopic (EM) level has hardly been examined. As it becomes increasingly evident that the function and physiological effectiveness of stress proteins are highly dependent on their spatial location and their associations with diverse regulator proteins, the demand for morphological studies which can identify their detailed distribution within the cells is evident. The reason for the practical lack of studies carried out at the EM level, lies in the shortage of reagents with suitable specificity and avidity necessary for this type of examination. To create such a reagent, a polyclonal antibody was raised using a recombinant truncated form of the inducible Hsp-72 protein. The antibody was extensively characterized, using different immunochemical methods to determine and verify its specificity, and then it was tried in ultrastructural examinations. Using the new antibody, it was possible to analyze the intracellular distribution of Hsp-72 with the immunogold technique. The localization of Hsp-72 was demonstrated directly at the ultrastructural level in the cytoplasm (especially at the cisterns of the RER), in the nucleus (mainly around the heterochromatic regions) and at both sides of the nuclear envelope close to the membrane pores. Apart from these localizations, Hsp-72 was found in several membrane bordered intracellular structures, which mainly belong to the endosomal-lysosomal system. We provide the first morphological verification of the appearance of Hsp-72 on the surface of the cells. Also novel is the indication, that the stress protein may recycle from the cell surface using a common route which includes coated pits and the endosomal system.
Starting Page	139
File Format	PDF
ISSN	14661268
e-ISSN	14661268
Journal	Cell Stress & Chaperones
Issue Number	2
Volume Number	4
Language	English
Publisher	Cell Stress Society International
Publisher Date	1999-06-01
Access Restriction	Open
Rights Holder	Cell Stress Society International
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Serum antibody titers against heat shock protein 27 are associated with the severity of coronary artery disease

Cloning, Expression, and Cell Localization of a Novel Small Heat Shock Protein Gene: BmHSP25.4

Regulation of Heat Shock Protein 90 ATPase Activity by Sequences in the Carboxyl Terminus

Glucose ingestion attenuates the exercise-induced increase in circulating heat shock protein 72 and heat shock protein 60 in humans

Quantitation and intracellular localization of the 85K heat shock protein by using monoclonal and polyclonal antibodies.

Purification of a 38-kDa Protein from Rabbit Reticulocyte Lysate Which Promotes Protein Renaturation by Heat Shock Protein 70 and Its Identification as δ-Aminolevulinic Acid Dehydratase and as a Putative DnaJ Protein

Heat shock-induced myocardial protection against ischemic injury: a role for Hsp 70?

Plasma heat shock protein 72 as a biomarker of sarcopenia in elderly people

Prostaglandin E2 Potentiates Heat Shock-Induced Heat Shock Protein 72 Expression in A549 Cells

Ultrastructural localization of Hsp-72 examined with a new polyclonal antibody raised against the truncated variable domain of the heat shock protein

Similar Documents

Serum antibody titers against heat shock protein 27 are associated with the severity of coronary artery disease

Cloning, Expression, and Cell Localization of a Novel Small Heat Shock Protein Gene: BmHSP25.4

Regulation of Heat Shock Protein 90 ATPase Activity by Sequences in the Carboxyl Terminus

Glucose ingestion attenuates the exercise-induced increase in circulating heat shock protein 72 and heat shock protein 60 in humans

Quantitation and intracellular localization of the 85K heat shock protein by using monoclonal and polyclonal antibodies.

Purification of a 38-kDa Protein from Rabbit Reticulocyte Lysate Which Promotes Protein Renaturation by Heat Shock Protein 70 and Its Identification as δ-Aminolevulinic Acid Dehydratase and as a Putative DnaJ Protein

Heat shock-induced myocardial protection against ischemic injury: a role for Hsp 70?

Plasma heat shock protein 72 as a biomarker of sarcopenia in elderly people

Prostaglandin E2 Potentiates Heat Shock-Induced Heat Shock Protein 72 Expression in A549 Cells

Ultrastructural localization of Hsp-72 examined with a new polyclonal antibody raised against the truncated variable domain of the heat shock protein