Heat shock proteins (HSPs) constitute a heterogeneous family of proteins involved in cell homeostasis. During cell life they are involved in harmful insults, as well as in immune and inflammatory reactions. It is known that they regulate gene expression, and cell proliferation, differentiation and death. HSP60 is a mitochondrial chaperonin, highly preserved during evolution, responsible of protein folding. Its function is strictly dependent on HSP10 in both prokaryotic and eukaryotic elements. We investigated the presence and the expression of HSP60 and HSP10 in a series of 20 normal human bone marrow specimens (NHBM) by the means of immunohistochemistry. NHBM showed no expression of HSP60, probably due to its being below the detectable threshold, as already demonstrated in other normal human tissues. By contrast, HSP10 showed a selective positivity for myeloid and megakaryocytic lineages. The positivity was restricted to precursor cells, while mature elements were constantly negative. We postulate that HSP10 plays a role in bone marrow cell differentiation other than being a mitochondrial co-chaperonin. The present data emphasize the role of HSP10 during cellular homeostasis and encourage further investigations in this field.

CAPPELLO F, TRIPODO C, FARINA F, FRANCO V, ZUMMO G (2004). HSP10 selective preference for myeloid and megakaryocytic precursors in normal human bone marrow. EUROPEAN JOURNAL OF HISTOCHEMISTRY, 48, 261-265.

HSP10 selective preference for myeloid and megakaryocytic precursors in normal human bone marrow

CAPPELLO, Francesco;TRIPODO, Claudio;FARINA, Felicia;FRANCO, Vito;ZUMMO, Giovanni
2004-01-01

Abstract

Heat shock proteins (HSPs) constitute a heterogeneous family of proteins involved in cell homeostasis. During cell life they are involved in harmful insults, as well as in immune and inflammatory reactions. It is known that they regulate gene expression, and cell proliferation, differentiation and death. HSP60 is a mitochondrial chaperonin, highly preserved during evolution, responsible of protein folding. Its function is strictly dependent on HSP10 in both prokaryotic and eukaryotic elements. We investigated the presence and the expression of HSP60 and HSP10 in a series of 20 normal human bone marrow specimens (NHBM) by the means of immunohistochemistry. NHBM showed no expression of HSP60, probably due to its being below the detectable threshold, as already demonstrated in other normal human tissues. By contrast, HSP10 showed a selective positivity for myeloid and megakaryocytic lineages. The positivity was restricted to precursor cells, while mature elements were constantly negative. We postulate that HSP10 plays a role in bone marrow cell differentiation other than being a mitochondrial co-chaperonin. The present data emphasize the role of HSP10 during cellular homeostasis and encourage further investigations in this field.
2004
CAPPELLO F, TRIPODO C, FARINA F, FRANCO V, ZUMMO G (2004). HSP10 selective preference for myeloid and megakaryocytic precursors in normal human bone marrow. EUROPEAN JOURNAL OF HISTOCHEMISTRY, 48, 261-265.
File in questo prodotto:
File Dimensione Formato  
OP 15. Cappello et al, EJH 2004.pdf

Solo gestori archvio

Dimensione 121.41 kB
Formato Adobe PDF
121.41 kB Adobe PDF   Visualizza/Apri   Richiedi una copia

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10447/21338
Citazioni
  • ???jsp.display-item.citation.pmc??? 11
  • Scopus 22
  • ???jsp.display-item.citation.isi??? 19
social impact