Regulatory effects of S-100 protein and parvalbumin on protein kinases and phosphoprotein phosphatases from brain and skeletal muscle

Abstract

In the eluted fractions of histone-treated crude extracts separated by Sephadex G-200 filtration, multiple protein kinase (PK) activities, including three from brain and two from skeletal muscle, were augmented by both S-100 protein and parvalbumin on the phosphorylation of endogenous substrates. One additional PK activity suppressed by both S-100 and parvalbumin was also found in muscle. In comparison, phosphoprotein phosphatases (PPase), which were also prepared by the same procedure of initial step of histone-treatment followed by the steps of Bio-Gel P-6DG for brain and DNA-cellulose for muscle, were all activated by S-100 while inhibited by parvalbumin and phosphatidylserine.

Perineuronal nets of extracellular matrix around parvalbumin‐containing neurons of the hippocampus

“…However, perineuronal nets avoid calretinin-positive neurons (Liith et al, 1992). Notwithstanding considerable effort, an effect of parvalbumin or calbindin D-28k (Blum et al, 1973;Kuo et al, 1986) on the activity of kinases or phosphatases has never been convincingly demonstrated. Further studies with modern, more refined techniques are warranted.…”

Histochemical Studies on the Camel Extraocular Muscles and Their Innervation

“…S-100 had many functions in cell-cell adhesion protein synthesis and energy metabolism excitation contraction and structure of biochemistry of the thick and thin filaments in skeletal muscle. S-100 protein has been reported to regulate protein kinase activity (Kuo et al, 1986a). Also, S -100 protein had detected in peripheral nerve cells.…”

Immunoreactivities of p11 and calcyclin in baker's yeast, wheat germ and lobster

“…These proteins play a versatile regulatory role in mammalian cells [1, [3][4][5][6][7][8][9][10][11][12][13][14][15].…”