Galactoglycerolipids of Mammalian Testis, Spermatozoa, and Nervous Tissue

Murray, Robert K.; Narasimhan, Rajagopolian; Levine, Mark; Pinteric, L.; Shirley, Margaret A.; Lingwood, Clifford A.; Schacter, Harry

doi:10.1021/bk-1980-0128.ch007

Cited by 21 publications

(15 citation statements)

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“…In this context it has been known for some time that surface glycoproteins responsible for cellular adhesion in a variety of different systems are often sulfated [102]. Of particular interest is the fact that the components of the ZP [9], as well as the sperm surface [103], are also highly sulfated in nature. Furthermore, early studies have confirmed the relevance of sulfated moieties in sperm-zona adhesion.…”

Section: Capacitationmentioning

confidence: 99%

New insights into the molecular mechanisms of sperm-egg interaction

Nixon

Aitken

McLaughlin

2007

Cell. Mol. Life Sci.

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At the moment of insemination millions of mammalian sperm cells are released into the female reproductive tract in order to find a single cell - the oocyte. The spermatozoa subsequently ignore the thousands of cells they make contact with during their journey to the site of fertilisation, until they reach the surface of the oocyte. At this point, they bind tenaciously to the acellular coat, known as the zona pellucida, that surrounds the oocyte and initiate the chain of cellular interactions that will culminate in fertilization. These exquisitely cell- and species-specific recognition events are among the most strategically important cellular interactions in biology. Understanding the cellular and molecular mechanisms that underpin them has implications for diagnosis of the aetiology of human infertility and the development of novel targets for fertility regulation. Herein, we describe two models indicating the plethora of highly orchestrated molecular interactions underlying successful sperm zona binding and sperm oocyte fusion.

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Section: Capacitationmentioning

confidence: 99%

New insights into the molecular mechanisms of sperm-egg interaction

Nixon

Aitken

McLaughlin

2007

Cell. Mol. Life Sci.

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“…Standards as in Figure 2a Figure 2a (4-8). Although SGG is only found in mammalian testes (Lingwood et al, 1981; radiochemical traces are also found in the brain; Murray et al, 1980), sulfogalactosphingolipids are found in the male germ cells of all species so far tested. Thus cartilagenous fish, amphibians, reptiles, and avian species contain SGC while bony fish contain sulfolactosylceramide in addition to SGC (Murray et al, 19801.…”

Section: Slip 1 Was Originally Isolated From the Sucroselatpjmentioning

confidence: 99%

Sulfogalactolipid binding protein SLIP 1: A conserved function for a conserved protein

Law

Itkonnen

Lingwood

1988

Journal Cellular Physiology

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We have studied the species and tissue expression of the 68kD sulfogalactolipid binding protein SLIP 1, originally detected in the male germ cells of the rat (Lingwood: Can. J. Biochem. Cell Biol., 63:1077-1085, 1985). Our results show that SLIP 1 has been highly conserved during evolution and is found in the testes of all vertebrates tested. In studies in the rat, we have found that SLIP 1 is, however, tissue restricted, being found only in the brain (also a major site of sulfogalactolipid biosynthesis) in addition to the testis. SLIP 1 was also detected in mammalian oocytes. The SLIP 1 species detected in brain and oocytes retain the sulfogalactolipid-binding characteristics of rat testicular SLIP 1, indicating that, in addition to immunological features, the glycolipid-binding function of SLIP 1 is conserved in these tissues.

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“…SGC is the major sulfoglycolipid of the kidney (23), brain, gastrointestinal tract (24,25), and endometrium (26). SGG (with or without SGC) is the major glycolipid of mammalian male germ cells (27) and has, together with an SGG-binding protein (28 -30) subsequently identified as the testes-specific hsc70 (18), been implicated in sperm/egg binding (31,32). SGC alone is found in the male germ cells of lower vertebrates (33) and in red and white blood cells (34).…”

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confidence: 99%

The ATPase Domain of hsp70 Possesses a Unique Binding Specificity for 3′-Sulfogalactolipids

Mamelak¹,

Lingwood

2001

Journal of Biological Chemistry

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The region(s) of hsp70 critical for sulfogalactolipid (SGL) recognition has been defined through deletion analysis and site-directed mutagenesis. Truncated polymerase chain reaction products of hsp70 generated N-terminal fragments of 43, 35, 29, and 22 kDa. The C terminus substrate-binding domain (28 kDa) was also expressed. The N-terminal ATPase domain (rP43) shared the binding specificity of hsp70, because only sulfogalactosyl ceramide and sulfogalactosyl glycerolipid were recognized by both TLC overlay and RELISA. The C-terminal domain showed no binding. SGL binding of rP29 and rP22 was severely reduced. The loss of SGL binding for rP35 by RELISA but not TLC overlay was considered as a function of receptor presentation. The truncation of rP43 to rP35 demonstrates that residues 318 -387 (the base of the ATP binding cleft) are critical for high affinity SGL binding. Mutagenesis showed that Arg 342 and Phe 198 are crucial for this process. SGL binding, mediated by these conserved residues within the ATPase domain of hsp70, implies that this binding specificity is evolutionarily conserved.Heat shock proteins of the 70-kDa family (hsp70) have traditionally been described as intracellular chaperones that facilitate protein folding (1), degradation (2), translocation across membranes (3), and disassembly of protein oligomers (4). These functions are driven by ATPase activity contained within the N-terminal domain of all hsp70 family members (5). Hsp70s have also been described on the surface of bacteria (6 -9), male germ cells (10), and carcinoma cell lines (11,12). The absence of extracellular ATP, however, likely renders the hsp70 chaperone function inoperative. Exogenous hsp70 has recently been shown to elicit a cytokine response after binding to the plasma membrane of monocytes (13) and to bind to the surface of antigen-presenting cells and undergo receptor-mediated endocytosis (14), consistent with a cell surface "receptor" for hsp70.We have previously described a novel function of hsp70 family members as cell surface-associated, SGL-specific adhesins. Anti-hsp70 antibodies prevent the attachment of mycoplasma (15), acid-stressed Helicobacter pylori (16), and temperaturestressed Hemophilus influenzae (17) to SGC.1 This SGL binding specificity was found to be shared by the bovine brain hsp70, recombinant mycoplasma hsp70s (15), and the recombinant testis-specific hsc70 (18).We have recently extended this survey to demonstrate that recombinant hsp70 family members from Chlamydia trachomatis (6), H. pylori (19), H. influenzae (17), Escherichia coli (20), and an hsp70-related extracellular domain from the egg receptor of the sea urchin, Strongylocentrotus purpuratus (21), all possess the same restricted "lectin" binding specificity for SGC and SGG in vitro. 2 We further found that heterogeneity within the lipid moiety of SGC can differentially modulate binding by prokaryote, as compared with eukaryote, hsp70s, which may reflect their different in vivo adhesin functions.Sulfogalactolipids are found in a variety of t...

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Galactoglycerolipids of Mammalian Testis, Spermatozoa, and Nervous Tissue

Cited by 21 publications

References 0 publications

New insights into the molecular mechanisms of sperm-egg interaction

New insights into the molecular mechanisms of sperm-egg interaction

Sulfogalactolipid binding protein SLIP 1: A conserved function for a conserved protein

The ATPase Domain of hsp70 Possesses a Unique Binding Specificity for 3′-Sulfogalactolipids

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