Raman spectroscopy and digital holography reveal visible light photodamage on human sperm cells

2016 ◽  
Author(s):  
A. De Angelis ◽  
M.A. Ferrara ◽  
G. Coppola ◽  
A.C. De Luca
Keyword(s):  
Raman Spectroscopy ◽  
Visible Light ◽  
Digital Holography ◽  
Human Sperm ◽  
Sperm Cells

scholarly journals Raman spectroscopy of DNA packaging in individual human sperm cells distinguishes normal from abnormal cells

2009 ◽  
Vol 2 (5) ◽  
pp. 322-332 ◽  
Author(s):  
Thomas Huser ◽  
Christine A. Orme ◽  
Christopher W. Hollars ◽  
Michele H. Corzett ◽  
Rod Balhorn
Keyword(s):  
Raman Spectroscopy ◽  
Human Sperm ◽  
Dna Packaging ◽  
Sperm Cells ◽  
Abnormal Cells ◽  
Individual Human

scholarly journals Sperm BerserKers

eLife ◽  
2013 ◽  
Vol 2 ◽  
Author(s):  
David E Clapham
Keyword(s):  
Ion Channel ◽  
Human Sperm ◽  
Potassium Ion ◽  
Sperm Cells ◽  
Potassium Ion Channel ◽  
Unusual Type

Human sperm cells rely on an unusual type of potassium ion channel.

scholarly journals Expression and function of ras proto-oncogene proteins in human sperm cells

1992 ◽  
Vol 102 (3) ◽  
pp. 487-494 ◽  
Author(s):  
R.K. Naz ◽  
K. Ahmad ◽  
P. Kaplan
Keyword(s):  
Sperm Cell ◽  
Acrosome Reaction ◽  
Cell Function ◽  
Beat Frequency ◽  
Human Sperm ◽  
Sperm Cells ◽  
Ras Protein ◽  
Head Displacement ◽  
Sperm Penetration ◽  
And Function

The presence and role of c-ras proteins were investigated in mature human sperm cells. The v-H-ras monoclonal antibody (mAb) against the c-ras protein, p21, reacted specifically with the acrosomal region of methanol-fixed as well as unfixed-live capacitated and non-capacitated human sperm cell in the indirect immunofluorescence technique. The v-H-ras mAb predominantly recognized c-ras protein of 21 kDa on the Western blot of lithium diiodosalicylate (LIS)-solubilized human sperm preparation. The incubation of sperm cells with v-H-ras mAb affected the sperm cell function in the human sperm penetration assay. The antibody significantly reduced the acrosome reaction and release of acrosin activity from the sperm cells. There was no effect of the mAb on percentage motility, although the mAb significantly affected various motility characteristics such as linearity, amplitude of lateral head displacement (ALH) and beat frequency, the motility parameters involved in the hyperactivation phenomenon of sperm cells leading to capacitation and acrosome reaction. These results suggest that the c-ras or c-ras-like proteins are present in mature sperm cell and may have a role in capacitation and/or acrosome reaction of human sperm cell.

scholarly journals Chemical UV Filters Mimic the Effect of Progesterone on Ca2+ Signaling in Human Sperm Cells

Endocrinology ◽  
2016 ◽  
Vol 157 (11) ◽  
pp. 4297-4308 ◽  
Author(s):  
A. Rehfeld ◽  
S. Dissing ◽  
N. E. Skakkebæk
Keyword(s):  
Human Sperm ◽  
Sperm Cells ◽  
Uv Filters

Human Sperm Cells

2002 ◽  
pp. 127-137
Author(s):  
Anita Rauch
Keyword(s):  
Human Sperm ◽  
Sperm Cells

Role of membrane phosphotyrosine proteins in human spermatozoal function

1991 ◽  
Vol 99 (1) ◽  
pp. 157-165
Author(s):  
R.K. Naz ◽  
K. Ahmad ◽  
R. Kumar
Keyword(s):  
Physiological State ◽  
Human Sperm ◽  
Kinase Assay ◽  
Relative Molecular Mass ◽  
Sperm Cells ◽  
Western Blots ◽  
Tyrosine Residues ◽  
Sperm Extract ◽  
32P Incorporation

The monoclonal anti-phosphotyrosine antibody (PTA) recognized proteins related to relative molecular mass regions of 94,000 +/− 3000 and 46,000 +/− 3000 Mr on Western blots of detergent-solubilized non-capacitated human sperm extract (HSE). The pattern of phosphorylation at tyrosine residues depended upon the physiological state of the sperm cells. At least six protein bands corresponding to four molecular regions of 94,000 +/− 3000, 46,000 +/− 3000, 25,000 +/− 7000 and 12,000 +/− 2000 Mr, respectively, were labeled with 32P when human sperm were capacitated in vitro; the proteins belonging to the former three regions were phosphotyrosine proteins as they were precipitable by PTA. In vitro kinase assay performed directly on HSE indicated autophosphorylation of proteins of the same four molecular regions, with the capacitated sperm preparations having 30% higher 32P incorporation into 94,000 +/− 3000 Mr proteins and 17% less incorporation into 12,000 +/− 2000 Mr proteins as compared to the non-capacitated sperm preparations. Both of these protein regions were also autophosphorylated at tyrosine residues when immunoprecipitated phosphotyrosine proteins were used for the kinase assay. Phosphorylation of tyrosine residues of 94,000 +/− 3000 Mr proteins was further stimulated by 1.38- to 1.46-fold in response to exposure to zona pellucida proteins, namely the porcine ZP3 and human zona proteins (HZP); the HZP induced the highest response. Immunofluorescence observations on fixed human sperm demonstrated that capacitation as well as exposure to zona proteins increased the degree of tyrosine-specific fluorescence per sperm cell as well as the number of sperm cells that showed fluorescence at the acrosomal region of the spermhead.(ABSTRACT TRUNCATED AT 250 WORDS)

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