1998
DOI: 10.1172/jci1614
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Extracellularly occurring histone H1 mediates the binding of thyroglobulin to the cell surface of mouse macrophages.

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Cited by 80 publications
(55 citation statements)
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“…Furthermore, the results of the in vitro functional tests (e.g., neurite outgrowth from cerebellar neurons, Schwann cell process formation and proliferation, as well as migration of neural progenitor cells) indicated that extracellular histone H1 interacts with PSA at the cell surface and that this interaction induces the observed effects of histone H1 on the investigated neural cells. Indications for the unusual extracellular location of histone H1, which was first identified as a nuclear protein, have been found in several other studies: histone H1 has been observed at the cell surface of cultured mouse cortical neurons (Bolton and Perry, 1997), human monocytes (Holers and Kotzin, 1985), activated human peripheral blood lymphocytes (Watson et al, 1995), cultured T-cells (Watson et al, 1995(Watson et al, , 1999, a macrophage cell line (Brix et al,1998), and skeletal muscle cells (Henriquez et al, 2002). So far, the mechanism(s) by which histone H1 crosses the membrane are not known.…”
Section: Discussionmentioning
confidence: 80%
See 1 more Smart Citation
“…Furthermore, the results of the in vitro functional tests (e.g., neurite outgrowth from cerebellar neurons, Schwann cell process formation and proliferation, as well as migration of neural progenitor cells) indicated that extracellular histone H1 interacts with PSA at the cell surface and that this interaction induces the observed effects of histone H1 on the investigated neural cells. Indications for the unusual extracellular location of histone H1, which was first identified as a nuclear protein, have been found in several other studies: histone H1 has been observed at the cell surface of cultured mouse cortical neurons (Bolton and Perry, 1997), human monocytes (Holers and Kotzin, 1985), activated human peripheral blood lymphocytes (Watson et al, 1995), cultured T-cells (Watson et al, 1995(Watson et al, , 1999, a macrophage cell line (Brix et al,1998), and skeletal muscle cells (Henriquez et al, 2002). So far, the mechanism(s) by which histone H1 crosses the membrane are not known.…”
Section: Discussionmentioning
confidence: 80%
“…It is also present extranuclearly (Parseghian and Luhrs, 2006) and even extracellularly at the surface of several cell types (Watson et al, 1995;Brix et al, 1998;Henriquez et al, 2002).…”
Section: Introductionmentioning
confidence: 99%
“…Thyroglobulin interactions with thyroid membranes have been observed for several years (Consiglio et al 1981). Several 'receptors' liable to mediate Tg binding to cell surfaces have been recently described: a receptor able to bind asialoagalacto Tg at acidic pH levels (Miquelis et al 1987); the protein disulfide isomerase (PDI) (Mezghrani et al 2000); histone H1 (Brix et al 1998); heparin (Marino et al 1999a); megalin (Zheng et al 1998, Marino et al 1999b; and rat hepatic lectin subunit of a rat asialoglycoprotein receptor (ASGPR) , Ulianich et al 1999. Some functions have been associated with various 'receptors': megalin was shown to be involved in transcytosis ; PDI was associated with Tg recycling (Miquelis et al 1987, Mezghrani et al 2000; histone H1 was involved in circulating Tg uptake by macrophages (Brix et al 1998); and a role was proposed for ASGPR in feedback regulation, ASGPR preventing thyroid-restricted gene expression under follicular Tg binding , Ulianich et al 1999.…”
Section: Introductionmentioning
confidence: 99%
“…However, some nuclear proteins are expressed on the cell surface and play alternative roles. For example, eukaryotic histone H1 on the cell membrane is identified as a receptor for thyroglobulin that is the precursor of thyroid hormones (16). High mobility group 1 protein is a eukaryotic nuclear protein associated with chromatin but also secreted in the extracellular milieu (17).…”
mentioning
confidence: 99%