Interleukin 1 receptors and biological responses.
Interleukin 1 (IL-1) is a polypeptide which possesses a wide variety of biological properties. IL-1 was originally studied as "endogenous pyrogen" and "leukocytic endogenous mediator" and more recently as "lymphocyte activating factor." Within a few minutes after intrav...
Autores principales: | , , , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Yale Journal of Biology and Medicine
1990
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2589311/ https://www.ncbi.nlm.nih.gov/pubmed/2144681 |
_version_ | 1782161093362188288 |
---|---|
author | Dinarello, C. A. Clark, B. D. Ikejima, T. Puren, A. J. Savage, N. Rosoff, P. M. |
author_facet | Dinarello, C. A. Clark, B. D. Ikejima, T. Puren, A. J. Savage, N. Rosoff, P. M. |
author_sort | Dinarello, C. A. |
collection | PubMed |
description | Interleukin 1 (IL-1) is a polypeptide which possesses a wide variety of biological properties. IL-1 was originally studied as "endogenous pyrogen" and "leukocytic endogenous mediator" and more recently as "lymphocyte activating factor." Within a few minutes after intravenous injection into experimental animals, IL-1 triggers events in the hypothalamus to initiate fever, slow-wave sleep, and the release of a variety of neuropeptides. The nature of the IL-1 receptors (IL-1R) is important to the understanding of IL-1's multiple action in mediating both neural and non-neural events. In this paper, the data are reviewed on the physical nature of the dominant, high-binding 80 kDa IL-1R isolated from murine T cells. In addition, newer studies demonstrate the existence of other IL-1 binding proteins which may participate as functional IL-1 receptors. These are a 68-75 kDa binding protein found on B cells and a 26-30 kDa binding protein found on T cells and mesangial cells. There is a considerable discrepancy between the number and affinities of the 80 kDa IL-1R and biological responses. Little is known about the relationship of the 68-75 or 26-30 kDa IL-R's biological responses. It is possible that, similar to neurotransmitter receptors, multiple chains of different binding proteins participate in the signal transduction of IL-1. The hydrolysis of non-phosphatidyl inositol membrane phospholipids plays an important role in responses to IL-1. |
format | Text |
id | pubmed-2589311 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1990 |
publisher | Yale Journal of Biology and Medicine |
record_format | MEDLINE/PubMed |
spelling | pubmed-25893112008-11-28 Interleukin 1 receptors and biological responses. Dinarello, C. A. Clark, B. D. Ikejima, T. Puren, A. J. Savage, N. Rosoff, P. M. Yale J Biol Med Research Article Interleukin 1 (IL-1) is a polypeptide which possesses a wide variety of biological properties. IL-1 was originally studied as "endogenous pyrogen" and "leukocytic endogenous mediator" and more recently as "lymphocyte activating factor." Within a few minutes after intravenous injection into experimental animals, IL-1 triggers events in the hypothalamus to initiate fever, slow-wave sleep, and the release of a variety of neuropeptides. The nature of the IL-1 receptors (IL-1R) is important to the understanding of IL-1's multiple action in mediating both neural and non-neural events. In this paper, the data are reviewed on the physical nature of the dominant, high-binding 80 kDa IL-1R isolated from murine T cells. In addition, newer studies demonstrate the existence of other IL-1 binding proteins which may participate as functional IL-1 receptors. These are a 68-75 kDa binding protein found on B cells and a 26-30 kDa binding protein found on T cells and mesangial cells. There is a considerable discrepancy between the number and affinities of the 80 kDa IL-1R and biological responses. Little is known about the relationship of the 68-75 or 26-30 kDa IL-R's biological responses. It is possible that, similar to neurotransmitter receptors, multiple chains of different binding proteins participate in the signal transduction of IL-1. The hydrolysis of non-phosphatidyl inositol membrane phospholipids plays an important role in responses to IL-1. Yale Journal of Biology and Medicine 1990 /pmc/articles/PMC2589311/ /pubmed/2144681 Text en |
spellingShingle | Research Article Dinarello, C. A. Clark, B. D. Ikejima, T. Puren, A. J. Savage, N. Rosoff, P. M. Interleukin 1 receptors and biological responses. |
title | Interleukin 1 receptors and biological responses. |
title_full | Interleukin 1 receptors and biological responses. |
title_fullStr | Interleukin 1 receptors and biological responses. |
title_full_unstemmed | Interleukin 1 receptors and biological responses. |
title_short | Interleukin 1 receptors and biological responses. |
title_sort | interleukin 1 receptors and biological responses. |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2589311/ https://www.ncbi.nlm.nih.gov/pubmed/2144681 |
work_keys_str_mv | AT dinarelloca interleukin1receptorsandbiologicalresponses AT clarkbd interleukin1receptorsandbiologicalresponses AT ikejimat interleukin1receptorsandbiologicalresponses AT purenaj interleukin1receptorsandbiologicalresponses AT savagen interleukin1receptorsandbiologicalresponses AT rosoffpm interleukin1receptorsandbiologicalresponses |