Plasma Proteins in Cancer

Winzler, Richard J.

doi:10.1016/s0065-230x(08)60010-x

Cited by 55 publications

(12 citation statements)

References 211 publications

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“…Cachexia is, in turn, seen to be associated with hypoalbuminemia, a feature which has been observed by several previous workers (Ariel, 1949;Winzler, 1953;Peden et al, 1957).…”

Section: Discussionsupporting

confidence: 74%

Mechanism of impaired glucose tolerance in patients with neoplasia

Jasani¹,

Donaldson²,

Ratcliffe³

et al. 1978

Br J Cancer

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Summary.-The disappearance rate (k) of i.v. glucose was measured in cachectic and non-cachectic cancer patients and tumour-free controls. The respective k values were found to be 106+027 (mean+s.d.), 164±034 and 163±023. Of the other parameters measured, only plasma albumin level was found to vary significantly amongst the 3 categories, the mean level being the lowest in cachectic cancer patients. The means of total plasma protein, fasting blood glucose and plasma liver enzyme concentrations were similar in the 3 groups. Glucagon, a potent insulin secretogogue, failed to augment the fasting insulin level in cachectic but did so in non-cachectic cancer patients. Taken together, the findings suggest that the reduced glucose tolerance in patients with neoplasia is due to impairment of insulin release exhibited predominantly by ill-nourished advanced cancer patients having a moderate to severe degree of hypoalbuminemia.

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“…Cachexia is, in turn, seen to be associated with hypoalbuminemia, a feature which has been observed by several previous workers (Ariel, 1949;Winzler, 1953;Peden et al, 1957).…”

Section: Discussionsupporting

confidence: 74%

Mechanism of impaired glucose tolerance in patients with neoplasia

Jasani¹,

Donaldson²,

Ratcliffe³

et al. 1978

Br J Cancer

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“…These have been found primarily in the quantitative and qualitative composition of the serum proteins (reviewed by Winzler, 1953, andPetermann, 1961). Changes in tumour sera which may cause agglutination of tumour cells have not previously been reported.…”

Section: Discussionmentioning

confidence: 99%

“…Thus Sato, Amizuka and Sato (1962) have found that the non-specific agglutination of kieselguhr by human serum is quantitatively inhibited by increasing additions of human seromucoid. It is established that in cancer there is an elevation in serum seromucoid (Winzler, 1953). If this component plays a role in the HeLa cell agglutination system, it is possible that failure to obtain agglutination in some cancer sera (Table I) may have been due to an excessive elevation of this serum component.…”

Section: Discussionmentioning

confidence: 99%

The Agglutination of Tumour Cells In Vitro by Sera from Tumour Patients and Pregnant Women

Tal¹,

Dishon²,

Gross³

1964

Br J Cancer

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IN the course of study on the possibility of autoimmune mechanisms against tumour, the level of circulating antibodies to the autologous tumour cells was estimated by cell agglutination titres according to a technique previously developed in this laboratory (Pikovski, Tal, Schlesinger and Margoliash, 1957). It was soon found that cross agglutination occurred. It appeared that the sera from tumour patients contained a factor (AF) which could cause agglutination of, and be adsorbed by, tumour cells from a variety of sources. This paper represents an analysis of this phenomenon. MATERIALS AND METHODS Cell preparationCell suspensions were prepared from some human tumours, several normal human tissues and some mouse tumours by a previously described technique (Pikovski, Tal, Schlesinger and Margoliash, 1957). Suspensions of tissue cultures of HeLa cervical carcinoma, KB buccal carcinoma and Chang normal liver cells were also used. The preparation of the tissue culture suspensions is given in the following detail using HeLa cultures as the example.HeLa cultures were grown in Eagle's lact-yeast medium plus 15 per cent of normal human serum and horse serum, respectively, in milk bottles. After 7-8 days of growth, the medium was pipetted off, and the cell layer washed with 10 ml. of warm (370 C.) phosphate-buffered saline (PBS). The PBS was replaced by 10 ml. of 0-02 per cent Ethylenediamine Tetracetic acid (EDTA) in PBS devoid of Ca and Mg, and the culture kept at 370 C. for [15][16][17][18][19][20] minutes. This procedure loosened the cells from the wall of the culture bottle and the EDTA cell suspension was transferred to a test tube. Clumps of cells were dispersed by repeated pipetting with a fine Pasteur pipette, taking care to avoid foaming. The suspension was then centrifuged at 500 r.p.m. for 5 minutes. The supernate was carefully removed so as not to disturb the cell pellet. The cells were then resuspended in 8 ml. of warm RBS and centrifuged as above. The washed cells were counted and suspended in sufficient normal saline to give a concentration of 4 x 106 cells per ml. Agglutination procedureSera were diluted fourfold with 0-2 M phosphate buffer (pH 7.0). The pH of the system was critical. 2 x 105 Cells were added to 0 4 ml. of serum dilutions.

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“…We assume that this increased amount of albumin is repaid from some reserves of this protein in these early stages. Good (Winzler, 1953) providing evidence that such a transformation may exist in other tumour tissues, too. For the early stages of tumour growth, however, a general mobilization of protein metabolism must be taken into account in explaining the higher turn-over rate of serum albumin.…”

Section: Discussionmentioning

confidence: 99%

Metabolism of Serum Albumin in Tumour-Bearing Rats

Hradec¹

1958

Br J Cancer

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Plasma Proteins in Cancer

Cited by 55 publications

References 211 publications

Mechanism of impaired glucose tolerance in patients with neoplasia

Mechanism of impaired glucose tolerance in patients with neoplasia

The Agglutination of Tumour Cells In Vitro by Sera from Tumour Patients and Pregnant Women

Metabolism of Serum Albumin in Tumour-Bearing Rats

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