Acid phosphatases

Bull, Heather

doi:10.1136/mp.55.2.65

Cited by 209 publications

(109 citation statements)

References 72 publications

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“…Acid phosphatase is the class of enzymes that catalyses the breakdown of phosphomonoesters (phosphoenolpyruvate, glycerophosphate, guanosine triphosphate, NADPH, phosphotyrosine, trehalose-6-phosphate etc.) under acidic conditions [17]. Two years later, the acid phosphatase from the culture filtrate protein fraction responsible for the observed activity was identified as a 28-kDa protein [18].…”

Section: Sapmmentioning

confidence: 99%

Bacterial Virulence Factors: Secreted for Survival

et al. 2016

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Virulence is described as an ability of an organism to infect the host and cause a disease. Virulence factors are the molecules that assist the bacterium colonize the host at the cellular level. These factors are either secretory, membrane associated or cytosolic in nature. The cytosolic factors facilitate the bacterium to undergo quick adaptive-metabolic, physiological and morphological shifts. The membrane associated virulence factors aid the bacterium in adhesion and evasion of the host cell. The secretory factors are important components of bacterial armoury which help the bacterium wade through the innate and adaptive immune response mounted within the host. In extracellular pathogens, the secretory virulence factors act synergistically to kill the host cells. In this review, we revisit the role of some of the secreted virulence factors of two human pathogens: Mycobacterium tuberculosis-an intracellular pathogen and Bacillus anthracis-an extracellular pathogen. The advances in research on the role of secretory factors of these pathogens during infection are discussed.

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Section: Sapmmentioning

confidence: 99%

Bacterial Virulence Factors: Secreted for Survival

et al. 2016

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“…Acid phosphatases catalyze the hydrolysis of phosphomonoesters at an acidic pH (9). Bacterial nonspecific acid phosphatases (NSAP) are subdivided into three classes (for a review, see reference 67).…”

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confidence: 99%

Moraxella catarrhalisSynthesizes an Autotransporter That Is an Acid Phosphatase

Hoopman

Wang²,

Brautigam

et al. 2008

J Bacteriol

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Moraxella catarrhalis O35E was shown to synthesize a 105-kDa protein that has similarity to both acid phosphatases and autotransporters. The N-terminal portion of the M. catarrhalis acid phosphatase A (MapA) was most similar (the BLAST probability score was 10 Initially thought to be a harmless commensal organism, Moraxella catarrhalis has gradually gained repute as an etiologic agent of at least two significant diseases in humans. This gram-negative, unencapsulated bacterium has been shown to colonize the upper airways of infants and very young children (14,15) and is one of the three most prominent causes of otitis media (45). Additionally, adults with chronic obstructive pulmonary disease are at risk for infectious exacerbations caused by M. catarrhalis (45,66). A recent study indicates that each year in the United States, as many as four million chronic obstructive pulmonary disease exacerbations may be attributed to M. catarrhalis (46).The secretion of proteins by gram-negative bacteria is a function necessary for numerous metabolic and physiologic processes. Five different secretion systems have been well characterized in bacteria (13), and a sixth has recently been described (44, 56). The type V secretion system has received increased attention in recent years (11,27,35,38). The absence of a requirement for energy coupling or accessory factors for successful protein secretion has resulted in this class of proteins being described as autotransporters. In gram-negative bacteria, autotransporters make up the largest family of outer membrane porins involved in protein translocation (12). The autotransporter secretion system was first described for the immunoglobulin A1 protease of Neisseria gonorrhoeae (54, 55), and subsequently, numerous autotransporters have been described for other gram-negative bacteria (25,27). A threedomain model for type V secretion systems has emerged, comprising (i) an amino-terminal leader peptide or signal sequence, (ii) the secreted mature protein (or passenger domain), and (iii) a C-terminal translocation domain responsible for the formation of a pore in the outer membrane to allow passage of the passenger domain to the cell surface (26).The passenger domains of previously described autotransporter systems have been shown to have widely different functions in gram-negative bacteria, including but not limited to proteolytic, adhesive, and cytotoxic activities (27). M. catarrhalis has been shown to synthesize at least three proteins (i.e., UspA1, UspA2, and Hag) that have been classified as trimeric autotransporters and one additional protein that is considered a conventional autotransporter (i.e., McaP) (for reviews, see references 11, 19, and 35). These four previously characterized M. catarrhalis autotransporters have been shown to be involved in adherence (1), serum resistance (6), binding of immunoglobulin D (18), autoaggregation (51), and lipolysis (68).Acid phosphatases catalyze the hydrolysis of phosphomonoesters at an acidic pH (9). Bacterial nonspecific acid phosphatases...

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“…Five important forms of AcPs are found in humans: prostatic, lysosomal, erythrocytic, macrophagic, and osteoclastic (Bull et al, 2002). These forms were detected in erythrocytes, leukocytes, platelets, liver, spleen, kidney, bone, and other tissues (Saftig et al, 1997;Cerri et al, 1999;Bull et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Expression of acid phosphatase in the seminiferous epithelium of vertebrates

Peruquetti¹,

Taboga²,

Azeredo-Oliveira³

2010

Genet. Mol. Res.

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ABSTRACT. Acid phosphatases (AcPs) are known to provide phosphate to tissues that have high energy requirements, especially during development, growth and maturation. During spermatogenesis AcP activity is manifested in heterophagous lysosomes of Sertoli cells. This phagocytic function appears to be hormone-independent. We examined the expression pattern of AcP during the reproductive period of four species belonging to different vertebrate groups: Tilapia rendalli (Teleostei, Cichlidae), Dendropsophus minutus (Amphibia, Anura), Meriones unguiculatus (Mammalia, Rodentia), and Oryctolagus cuniculus (Mammalia, Lagomorpha). To demonstrate AcP activity, cryosections were processed for enzyme histochemistry by a modification of the method of Gömöri. AcP activity was similar in the testes of these four species. Testes of T. rendalli, D. minutus and M. unguiculatus showed an intense reaction in the Sertoli cell region. AcP activity was detected in the testes of D. minutus and O. cuniculus in seminiferous epithelium regions, where cells are found in more advanced stages of development. The seminiferous epithelium of all 621 ©FUNPEC-RP www.funpecrp.com.br Genetics and Molecular Research 9 (2): 620-628 (2010) Expression of acid phosphatase in the testes of vertebrates four species exhibited AcP activity, mainly in the cytoplasm of either Sertoli cells or germ cells. These findings reinforce the importance of AcP activity during the spermatogenesis process in vertebrates.

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Acid phosphatases

Cited by 209 publications

References 72 publications

Bacterial Virulence Factors: Secreted for Survival

Bacterial Virulence Factors: Secreted for Survival

Moraxella catarrhalisSynthesizes an Autotransporter That Is an Acid Phosphatase

Expression of acid phosphatase in the seminiferous epithelium of vertebrates

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