Molecular cloning, characterization, and differential expression pattern of mouse lung surfactant convertase

Krishnasamy, S.; Teng, Andelle L.; Dhand, Rajiv; Schultz, Richard M.; Gross, Nicholas J.

doi:10.1152/ajplung.1998.275.5.l969

Cited by 18 publications

(24 citation statements)

References 17 publications

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“…More specific roles for mammalian CES have been described, including the activation of lung surfactant (Krishnasamy et al, 1998); the detoxification of organophosphate and carbamate poisons (Jakonivic et al, 1996; Satoh and Hosokawa, 1998); the activation of several prodrugs used in treating various diseases such as influenza (He et al, 1999), cancer (Humerickhouse et al, 2000; Ohtsuka et al, 2003; Tabata et al, 2004) and high blood pressure (Takai et al, 1997); providing additional metabolic capacity as lipid hydrolases for neutral fats and phopholipids in tissues of the body (Mentlein et al, 1988; Ghosh et al, 1995; Tsujita and Okuda, 1993; Okazaki et al, 2006); and contributing to glucocorticosteroid drug activation within bronchial cells following prodrug inhalation (Mutch et al, 2007). …”

Section: Ces5 Functional Aspectsmentioning

confidence: 99%

“…Carboxylesterases (CES; E.C.3.1.1.1) catalyse hydrolytic and transesterification reactions using a broad range of substrates, detoxify organophosphates, carbamate compounds and insecticides (Ahmad & Forgash, 1976; Leinweber, 1987; Satoh and Hosokawa, 1998; Satoh et al, 2002; Redinbo and Potter, 2005), catalyse several cholesterol and fatty acid metabolic reactions (Tsujita and Okuda, 1993; Becker et al, 1994; Diczfalusy et al, 2001; Dolinsky et al, 2001), and facilitate the conversion of lung alveolar surfactant (Krishnasamy et al, 1998; Ruppert et al, 2006). CES is also involved in the biotransformation of many drugs and prodrugs (Ahmad et al, 1999; He et al, 1995; Imai et al, 2003; Ohtsuka et al, 2003; Imai, 2006; Mutch et al, 2007), anti-tumor drugs (Humerickhouse et al, 2000; Xu et al, 2002; Tabata et al, 2004) and narcotics, such as cocaine and heroine (Pindel et al, 1997), and has been linked with the assembly of very-low density lipoproteins in liver (Wang et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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Mammalian carboxylesterase 5: Comparative biochemistry and genomics

Holmes

Cox

VandeBerg

2008

Comparative Biochemistry and Physiology Part D: Genomics and Pr

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Carboxylesterase 5 (CES5) (also called cauxin or CES7) is one of at least five mammalian CES gene families encoding enzymes of broad substrate specificity and catalysing hydrolytic and transesterification reactions. In silico methods were used to predict the amino acid sequences, secondary structures and gene locations for CES5 genes and gene products. Amino acid sequence alignments of mammalian CES5 enzymes enabled identification of key CES sequences previously reported for human CES1, as well as other sequences that are specific to the CES5 gene family, which were consistent with being monomeric in subunit structure and available for secretion into body fluids. Predicted secondary structures for mammalian CES5 demonstrated significant conservation with human CES1 as well as distinctive mammalian CES5 like structures. Mammalian CES5 genes are located in tandem with the CES1 gene(s), are transcribed on the reverse strand and contained 13 exons. CES5 has been previously reported in high concentrations in the urine (cauxin) of adult male cats, and within a protein complex of mammalian male epididymal fluids. Roles for CES5 may include regulating urinary levels of male cat pheromones; catalysing lipid transfer reactions within mammalian male reproductive fluids; and protecting neural tissue from drugs and xenobiotics.

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Section: Ces5 Functional Aspectsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Mammalian carboxylesterase 5: Comparative biochemistry and genomics

Holmes

Cox

VandeBerg

2008

Comparative Biochemistry and Physiology Part D: Genomics and Pr

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“…Concerning the latter, the requirement of an enzymatic activity was proposed on the basis of inhibitor studies employing serine protease inhibitors [32]. A diisopropylfluorophosphate-binding protein, later named 'convertase', was isolated from BALF, purified, and characterized as a member of the carboxylesterase family [33,34]. The physiologic substrate of the esterase, however, is presently unknown.…”

Section: Alteration Of the Pulmonary Surfactant System In Acute Respimentioning

confidence: 99%

Surfactant alteration and replacement in acute respiratory distress syndrome

et al. 2001

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Introduction Acute respiratory distress syndromeThe acute respiratory distress syndrome (ARDS) describes an overwhelming inflammatory reaction within the pulmonary parenchyma leading to life-threatening disturbances in pulmonary vasomotion, alveolar ventilation, and gas exchange. Originally, this syndrome was described in 1967 by Ashbaugh and collegues [1]. According to the recent American-European Consensus Conference [2], ARDS is defined by an acute onset (catastrophic event), an oxygenation index (ratio of the partial pressure of arterial oxygen to the fraction of inspired oxygen [PaO 2 /FiO 2 ]) < 200 mmHg, bilateral infiltrates on chest radiography, and a pulmonary capillary wedge pressure <18 mmHg or absence of clinical evidence for left-sided heart failure. When the PaO 2 /FiO 2 ratio is between 200 and 300 mmHg and the other abovementioned criteria are met, the term 'acute lung injury' (ALI) should be used instead of ARDS. ARDS is a frequent disease (incidence between 13. AbstractThe acute respiratory distress syndrome (ARDS) is a frequent, life-threatening disease in which a marked increase in alveolar surface tension has been repeatedly observed. It is caused by factors including a lack of surface-active compounds, changes in the phospholipid, fatty acid, neutral lipid, and surfactant apoprotein composition, imbalance of the extracellular surfactant subtype distribution, inhibition of surfactant function by plasma protein leakage, incorporation of surfactant phospholipids and apoproteins into polymerizing fibrin, and damage/inhibition of surfactant compounds by inflammatory mediators. There is now good evidence that these surfactant abnormalities promote alveolar instability and collapse and, consequently, loss of compliance and the profound gas exchange abnormalities seen in ARDS. An acute improvement of gas exchange properties together with a far-reaching restoration of surfactant properties was encountered in recently performed pilot studies. Here we summarize what is known about the kind and severity of surfactant changes occuring in ARDS, the contribution of these changes to lung failure, and the role of surfactant administration for therapy of ARDS.

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“…CES also catalyses several lipid metabolic reactions (Tsujita and Okuda, 1993; Becker et al, 1994; Diczfalusy et al, 2001; Dolinsky et al, 2001), facilitates the conversion of lung alveolar surfactant (Krishnasamy et al, 1998; Ruppert et al, 2006) and is involved in the assembly of very-low density lipoproteins in liver (Wang et al, 2007). …”

Section: Introductionmentioning

confidence: 99%

A new class of mammalian carboxylesterase CES6

Holmes

Cox

VandeBerg

2009

Comparative Biochemistry and Physiology Part D: Genomics and Pr

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Mammalian carboxylesterases (CES) exhibit broad substrate specificities, catalyse hydrolytic and transesterification reactions with a wide range of drugs and xenobiotics and are widely distributed in the body. Four CES classes have been previously described, namely CES1 (major liver form); CES2 (major intestinal form); CES3 (highest activity in the colon); and CES5, a secreted enzyme found in mammalian kidney and male reproductive fluids. In silico methods were used to predict the amino acid sequences, structures and gene locations for a new class of CES genes and proteins, designated as CES6. Mammalian CES6 amino acid sequence alignments and predicted secondary and tertiary structures enabled the identification of key CES sequences previously reported for human CES1, but with CES6 specific sequences and properties: high isoelectric points (pI values of 8.8 -9.4 compared with 5.4 -6.2 for human CES1, CES2, CES3 and CES5); being predicted for secretion into body fluids compared with human CES1, human CES2 and CES3, which are membrane bound; and having Asn or Glu residues at the predicted CES1 Z-site for which a Gly residue plays a major role in cholesterol binding. Mammalian CES6 genes are located in tandem with CES2 and CES3 genes, are transcribed on the positive DNA strand and contain 14 exons. Human and mouse CES6-like transcripts have been previously reported to be widely distributed in the body but are localized in specific regions of the brain, including the cerebellum. CES6 may play a role in the detoxification of drugs and xenobiotics in neural and other tissues of the body and in the cerebrospinal fluid.

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Molecular cloning, characterization, and differential expression pattern of mouse lung surfactant convertase

Cited by 18 publications

References 17 publications

Mammalian carboxylesterase 5: Comparative biochemistry and genomics

Mammalian carboxylesterase 5: Comparative biochemistry and genomics

Surfactant alteration and replacement in acute respiratory distress syndrome

A new class of mammalian carboxylesterase CES6

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