Mini Review: The Forensic Value of Heat Shock Proteins

Forensic pathologists are routinely confronted with unclear causes of death or related findings. In some instances, difficulties arise in relation to questions posed by criminal investigators or prosecutors. Such scenarios may include questions about wound vitality or cause of death where typical or landmark findings are difficult to ascertain. In addition to the usual examinations required to clarify unclear causes of death or address specific questions, immunohistochemistry and genetic analyses have become increasingly important techniques in this area since their establishment last century. Since then, many studies have determined the usefulness and significance of immunohistochemical and genetic investigations on cellular structures and proteins. For example, these proteins include heat shock proteins (Hsp), which were first described in 1962 and are so called based on their molecular weight. They predominantly act as molecular chaperones with cytoprotective functions that support cell survival under (sub) lethal conditions. They are expressed in specific cellular compartments and have many divergent functions. Central family members include, Hsp 27, 60, and 70. This mini review investigates recent research on the Hsp family, their application range, respective forensic importance, and current limitations and provides an outlook on possible applications within forensic science.

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Interaction of Plasminogen and Angiostatin with Heat Shock Proteins.

Blood ◽

10.1182/blood.v108.11.1622.1622 ◽

2006 ◽

Vol 108 (11) ◽

pp. 1622-1622

Author(s):

Anil K. Dudani ◽

Jelica Mehic ◽

Anthony Martyres

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Dependent Manner ◽

Hsp 70 ◽

Molar Excess ◽

Hsp 27 ◽

Human Plasminogen ◽

Shock Proteins ◽

Dose Dependent ◽

Mcf 7

Abstract Previous studies from this laboratory have demonstrated that plasminogen and angiostatin bind to endothelial cell (EC) surface-associated actin via their kringles in a specific manner. Heat shock proteins (hsps) like hsp 27 are constitutively expressed by vascular ECs and regulate actin polymerization, cell growth and migration. Since many hsps have also been found to be highly abundant on cell surfaces and there is evidence that bacterial surface hsps may interact with human plasminogen, the purpose of this study was to determine whether human plasminogen and angiostatin would interact with human hsps. ELISAs were developed in our laboratory to assess these interactions. It was observed that plasminogen bound to hsps 27, 60 and 70. In all cases, binding was inhibited (85–90%) by excess (50 mM) lysine indicating kringle involvement. Angiostatin predominantly bound to hsp 27 and to hsp 70 in a concentration- and kringle-dependent manner. As observed previously for actin, there was dose-dependent inhibition of angiostatin’s interaction with hsp 27 by plasminogen. In addition, thirty-fold molar excess actin inhibited (up to 50%), the interaction of plasminogen with all hsps. However, thirty-fold molar excess actin could only inhibit the interaction of angiostatin with hsp 27 by 15–20%. FACS analyses indicated the presence of hsps 27, 60 and 70 on the surface of MCF-7 breast cancer cells but not on human umbilical vein ECs. Polyclonal antibodies to hsp 27 significantly inhibited the interaction of plasminogen and angiostatin with MCF-7 surface-associated hsp27 in a dose-dependent manner. Collectively, these data indicate that while plasminogen interacts specifically with hsp 27, 60 and 70, angiostatin interacts predominantly with hsp 27 and to some extent with hsp 70; plasminogen only partially displaces angiostatins binding to hsp 27; actin only partially displaces plasminogen/angiostatin binding to hsps and surface-associated hsp 27 can mediate the binding of both plasminogen and angiostatin to MCF-7 cells.

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Expression of heat shock proteins (hsp) 27 and 70 in various organ systems in cases of death due to fire

International Journal of Legal Medicine ◽

10.1007/s00414-014-0994-0 ◽

2014 ◽

Vol 128 (6) ◽

pp. 967-978 ◽

Cited By ~ 10

Author(s):

E. Doberentz ◽

L. Genneper ◽

D. Böker ◽

E. Lignitz ◽

B. Madea

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Hsp 27 ◽

Organ Systems ◽

Shock Proteins

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Heat shock proteins on beef quality

Pesquisa Agropecuária Brasileira ◽

10.1590/s0100-204x2018000100010 ◽

2018 ◽

Vol 53 (1) ◽

pp. 90-96

Author(s):

Cristina Tschorny Moncau ◽

Alessandra Fernandes Rosa ◽

Joanir Pereira Eler ◽

Júlio César de Carvalho Balieiro

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

South African ◽

Aging Time ◽

Meat Quality ◽

Meat Tenderness ◽

Beef Quality ◽

Longissimus Dorsi Muscle ◽

Hsp 27 ◽

Shock Proteins

Abstract: The objective of this work was to quantify heat shock proteins (HSP) 27 and 70 in the Longissimus dorsi muscle of cattle during aging and to check their potential as biomarkers for meat quality. A total of 191 steers ½ South African Simmental x ½ Nellore (16-18 months, 391.7±99.7 kg), castrated, and feedlot finished were used. Meat quality was measured by pH, color, cooking loss, and shear force (SF) at 1 and 14 days of aging time. HSP27 and HSP70 were quantified according to the SF values in the more and less tender meat groups, with 20 samples each, for each aging time. HSP27 concentrations in more and less tender meat decrease from 1 to 14 days of aging, and do not differ when evaluated at the same period. HSP70 concentrations in more tender meat increase during aging, and, in less tender meat, there is no difference between periods or at the same period. The correlations between the HSP27 and HSP70 concentrations and meat quality characteristics are low for South African Simmental x Nellore, which indicate the low potential of HSP as biomarkers for these traits, especially for meat tenderness.

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