An Antiagglutinic Factor in Mammalian Sperm Plasm

Lindahl, Per Eric; Kihlström, J. E.

doi:10.1016/s0015-0282(16)31624-7

Cited by 35 publications

(20 citation statements)

References 5 publications

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“…The present experiments on agglutination have been performed in the same manner as described earlier (see Lindahl & Kihlström, 1954a;Lindahl & Nilsson, 1954 (Lindahl & Kihlström, 1952b, 1954a; later ascorbic acid was also tried for the reduction of female antagglutin (see Lindahl & Nilsson, 1957). In this communication ergothioneine and sulphite are also included, the three last mentioned substances as well as glutathione being known to occur naturally in the seminal plasma of different mammals (Mann, 1954), whereas ascorbic acid is known also to occur in the tissue of the Fallopian tubes (Joël, 1941 ;Rodel & Karg, 1955).…”

Section: Methodsmentioning

confidence: 99%

“…3). Ergothioneine occurs in high concentrations in the seminal vesicle secretion of the boar (Mann, 1954 The ability to stick to the sperm cell surface is lost when the antagglutin is transformed into its oxidized form (Lindahl & Kihlström, 1954a). This fact is made use of in the method for quantitative determination of male antagglutin, elaborated by Lindahl, Kihlström & Ross (1957) in which hydrogen peroxide is used as the oxidizing agent.…”

Section: Methodsmentioning

confidence: 99%

“…This iso-agglutination is generally counter¬ acted and abolished by factors in the seminal plasma (Lindahl & Kihlström, 3 1952b;1954a), and in secretions of the female genital tract (Lindahl & Kihlström, 1952b;Lindahl & Nilsson, 1954;Lindahl, Ingelman-Sundberg, Furuhjelm & Nilsson, 1956;Ingelman-Sundberg & Lindahl, 1958). Sub¬ stances having this ability have been termed sperm antagglutins.…”

Section: Introductionmentioning

confidence: 99%

“…Sub¬ stances having this ability have been termed sperm antagglutins. The male substance is formed in the prostatic gland (cattle, man) and has been isolated from semen (Lindahl & Kihlström, 1954a). Sperm anti-agglutinic activity has been found in growing follicles, in tubai secretions at oestrus and after ovulation (rabbit, man, cattle), and in cervical secretions at ovulation (man, cattle).…”

Section: Introductionmentioning

confidence: 99%

“…Soon after the discovery of the sperm antagglutins, it was realized that the biological activity of these substances is limited to their reduced form (Lindahl & Kihlström, 1952b, 1954a At the same time, however, washing causes some kind of damage, rendering the agglutination of a smaller fraction of spermatozoa irreversible ; this agglu¬ tination which is resistant to high concentrations of active antagglutin, will be referred to as 'residual agglutination' ; the term 'agglutination from washing' is used for the total agglutination after washing.…”

Section: Introductionmentioning

confidence: 99%

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Some Factors Influencing the Biological Activity of Sperm Antagglutins

Lindahl¹

1960

Reproduction

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Some Factors Influencing the Biological Activity of Sperm Antagglutins

Lindahl¹

1960

Reproduction

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Maturation antigen of the mouse sperm flagellum. I. Analysis of its secretion, association with sperm, and function

1988

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We report here recent findings on the sperm maturation antigen SMA4, which is secreted by holocrine cells of the distal caput epididymis and binds to the flagellar surface of mouse sperm during epididymal transit. Washed sperm from the caput and corpus epididymides of mice were examined by immunofluorescence and SDS-PAGE using wheat germ agglutinin, which binds specifically to SMA4 as a primary probe. Results indicate that sperm first exhibit WGA reactivity on their flagellae in the region of the distal caput, and that the appearance of WGA receptors is due to the binding of a 54-Kd glycoprotein (SMA4) to the cell surface. Extracts of epididymis containing SMA4 were tested for their ability to bind to the surfaces of caput and corpus sperm. Caput sperm surfaces bound SMA4 in a temperature-independent manner, and binding occurred in the presence of enzyme inhibitors, suggesting a nonenzymatic process. Biochemical studies revealed that SMA4 contains disulfide bonds which stabilize it on the sperm surface and restrict its mobility. Terminal carbohydrate residues of the molecule are sialic acids. The addition of SMA4 to caput sperm flagellae prevented tail-to-tail agglutination, normally seen when caput sperm are diluted into saline; and SMA4 was able to disperse clumps of agglutinated caput sperm. The data suggest that a primary function of SMA4 is to prevent tail-to-tail agglutination of sperm during storage in the epididymis.

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Chemical N‐desulfation of heparin negates its ability to capacitate bovine spermatozoa

Rl²

1989

Gamete Research

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Heparin specifically and saturably binds to bovine spermatozoa and stimulates capacitation as assessed by the ability of spermatozoa to undergo a zona pellucida-induced acrosome reaction (AR) in vitro. However, the structural features of heparin important for capacitation are poorly understood. The purpose of this study was to determine the importance of the sulfate content of heparin for its potency to bind to bull spermatozoa and promote agglutination and capacitation. The pyridine salt of heparin was N-desulfated, which reduced its mean sulfate content from 19.7% to 11.6%. The N-desulfated heparin was then resulfated by incubation with trimethylamine sulfur trioxide for 6, 12, or 24 hr, raising sulfate to original concentrations. Heparin but not N-desulfated heparin competed with [3H]-heparin to bind to spermatozoa. Heparin at 11.6 micrograms/ml reduced [3H]-heparin binding by half when competing with a saturating concentration of the radiolabeled compound (12 micrograms/ml). N-desulfated heparin did not displace [3H]-heparin. Heparin, resulfated 6 hr or 12 hr, was equal to native heparin in binding potency. Heparin at 50, 100, or 250 micrograms/ml caused more than 40% of the cells to head-to-head agglutinate in aggregates of 8 or more. N-desulfated heparin did not cause agglutination. After spermatozoa were incubated with 0, 5, 10, 50, 100, or 250 micrograms/ml of heparin for 4 hr, 100 micrograms/ml of lysophosphatidylcholine (LPC)-induced AR within 20 min in 21.3, 37.7, 27.8, 45.3, 54.2, or 42.5% of the cells, respectively. Sperm exposed to the same concentrations of N-desulfated heparin exhibited AR of 17.7, 27.3, 24.3, 22.5, 27.7, or 33.8%, respectively, following exposure to LPC. Resulfated heparin did not agglutinate or capacitate spermatozoa. In conclusion, N-desulfation of heparin abolished heparin's ability to bind to, agglutinate, and capacitate bovine spermatozoa. Resulfation of N-desulfated heparin restored binding activity but not agglutination or capacitation activity.

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An Antiagglutinic Factor in Mammalian Sperm Plasm

Cited by 35 publications

References 5 publications

Some Factors Influencing the Biological Activity of Sperm Antagglutins

Some Factors Influencing the Biological Activity of Sperm Antagglutins

Maturation antigen of the mouse sperm flagellum. I. Analysis of its secretion, association with sperm, and function

Chemical N‐desulfation of heparin negates its ability to capacitate bovine spermatozoa

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