Alkaline Phosphatase High But Everything Else Normal

Alkaline Phosphatase High But Everything Else Normal – Personalized dietary recommendations based on individual postprandial glycemic response improve glycemic indices and PROMs in patients with type 2 diabetes: a real-world evaluation

Time to revitalize bone biopsy with histomorphometric analysis in chronic kidney disease (CKD): moving from skepticism to pragmatism

Alkaline Phosphatase High But Everything Else Normal

Alkaline Phosphatase High But Everything Else Normal

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Parameter Tuesday: Alkaline Phosphatase

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Algorithm For Evaluation Of An Elevated Alkaline Phosphatase Level….

Alkaline phosphatase: an old friend as a target for cardiovascular disease and bone mineral management in chronic kidney disease

Author: Mathias Haarhaus Mathias Haarhaus Scilit Google Scholar View publications 1, 2, Giuseppe Cianciolo Giuseppe Cianciolo Scilit Google Scholar View publications 3, Simona Barbuto Simona Barbuto Scilit Google Scholar View publications 3, Gaetano La Manna Gaetano La Manna Scilit Google Scholar View publications 3, Lorenzo Gasperoni Lorenzo Gasperoni Scilit Google Scholar View publications 4, Giovanni Tripepi Giovanni Tripepi Scilit Google Scholar View publications 5, Mario Plebani Mario Plebani Scilit Google Scholar View publications Publications 6 , Maria Fusaro Maria Fusaro Scilit Google Scholar View publications 7, 8, *, † and Per Magnusson Per Magnusson Scilit Google Scholar View publications 9, *, †

Division of Nephrological Medicine, Faculty of Clinical Sciences, Interventions and Technology, Karolinska Institutet, Karolinska University Hospital, SE-14186 Stockholm, Sweden

Alkaline Phosphatase High But Everything Else Normal

Department of Nephrology, Dialysis and Kidney Transplantation, IRCCS-Azienda Ospedaliero-Universitaria di Bologna, Alma Mater Studiorum University of Bologna, 40126 Bologna, Italy

Guidelines On The Management Of Abnormal Liver Blood Tests

Received: April 20, 2022 / Revised: May 12, 2022 / Accepted: May 17, 2022 / Published: May 19, 2022

(This article is part of the Special Issue Nutrition for Bone and Vascular Health: A Journey from Pathophysiology to Treatment)

Alkaline phosphatase (ALP) is an evolutionarily conserved enzyme and a widely used biomarker in clinical practice. Tissue-nonspecific alkaline phosphatase (TNALP) is one of four human isoenzymes that, after post-translational modifications, are expressed as distinct TNALP isoforms, mainly in bone, liver and kidney tissues. In addition to their well-known effects on bone mineralization, bone ALP (BALP) isoforms (B/I, B1, B1x, and B2) are also involved in the pathogenesis of ectopic calcifications. This narrative review summarizes the latest clinical research and mechanisms linking ALP and BALP to inflammation, metabolic syndrome, vascular calcification, endothelial dysfunction, fibrosis, cardiovascular disease, and mortality. The relationship between ALP, vitamin K, bone metabolism and fracture risk in patients with chronic kidney disease (CKD) was also discussed. Recent advances in various pharmacological strategies that have the potential to modulate ALP expression directly and indirectly in CKD-mineral and bone diseases (CKD-MBD) are highlighted, e.g., epigenetic modulation, phosphate binders, calcimimetics, vitamin D, and other anticancer drugs. -treatment of fractures. We conclude that substantial evidence for ALP as a pathogenic factor and risk marker in CKD-MBD supports the inclusion of specific ALP treatment targets in clinical guidelines. Although a target of less than 120 U/L is associated with improved survival, further experimental and clinical studies should explore interventional strategies with optimal risk-benefit profiles. The future looks very promising in terms of innovative drug therapies that modulate ALP.

Bone alkaline phosphatase; bone fracture; bone turnover; cardiovascular disease; end-stage renal disease; risk of fracture; intestinal alkaline phosphatase; vascular calcification; vitamin K; vitamin K-dependent proteins

High Serum Alkaline Phosphatase Levels, A Study In 181 Thai Adult Hospitalized Patients

Alkaline phosphatase (ALP; EC is a highly conserved enzyme that catalyzes the hydrolysis of phosphomonoesters, e.g. the endogenous inorganic substrate pyrophosphate (PPi), with optimal activity at alkaline pH values. Four ALP isoenzymes are expressed in humans: tissue-nonspecific ALP (TNALP, or liver/bone/kidney ALP), intestinal ALP (IALP), placental ALP (PALP, or PLAP), and germ cell ALP (GCALP, or placenta-like). CRAG). Tissue-specific ALPs (i.e. IALP, PALP and GCALP) are located on chromosome 2, bands q34.2–q37, with 90–98% sequence identity (Figure 1) [1]. The TNALP ALPL gene is located on the short arm of chromosome 1, band 1p36.12, with approximately 50% homology to three tissue-specific ALPs and is at least five times larger, mainly due to differences in intron size [2, 3, 4]. As the “tissue-nonspecific” isozyme name suggests, TNALP is ubiquitously expressed and modified by post-translational glycosylation processes, becoming isoforms that provide significant proteomic diversity and specificity for different tissues and cells. The highest levels of human TNALP isoforms are expressed in bone, liver, and kidney tissues [1]; with neutrophil granulocytes [5], brain [6] and vascular cells [7] as secondary sources of TNALP activity.

All ALP isozymes function as homodimers and are attached to the outer cell membrane (i.e., ALP is an ectozyme) via a glycosylphosphatidylinositol (GPI) anchor. Release of soluble (anchor-free) ALP into the circulation occurs through cleavage by GPI-specific phospholipase D [8, 9, 10]. Several families of GPI proteins are known, but circulating GPI-specific phospholipase D is not active against GPI-anchored proteins on the surface of intact cells [11, 12]. The mechanistic basis of targeting and subsequent activation for cleavage of GPI-linked proteins remains elusive, although some inhibitory elements and activators have been described [13].

The ALP hodimer has two active site regions, and each site is dependent on a metal triplet containing one Mg

Alkaline Phosphatase High But Everything Else Normal

Ions. Zinc can bind to all three sites, but binds particularly strongly to two of them, while magnesium comes second to the ALP monomer [14, 15]. No ALP has been shown to be enzymatically active in the metal-free state. The fourth metal binding site, occupied by one Ca

Pdf) Elevated Alkaline Phosphatase In Children: An Algorithm To Determine When A “wait And See” Approach Is Optimal

Ion and present in all human ALP isozymes, is another important structural feature. Although distant from the active site, several clinically serious mutations in TNALP occur close to this calcium binding site [16, 17]. The functional implications of this non-catalytic calcium binding, however, remain to be elucidated.

In serum, bone ALP (BALP) and liver ALP isoforms are the most abundant TNALP isoforms, in a ratio of approximately 1:1, accounting for over 90% of total ALP activity [18]. The remaining circulating ALP activity of 1–10% is mainly attributed to IALP [19]. Over the years, several different analytical methods have been described for the separation and quantification of ALP and TNALP isozymes in serum [20]. In particular, the development of commercial immunoassays for the determination of BALP in serum has improved suitability and availability in routine clinical examinations and research. While this is a positive development, users should be aware that these immunoassays have some weaknesses regarding standardization, inter-method variability, and cross-reactivity with hepatic ALP epitopes [20, 21, 22].

Four different BALP isoforms (B/I, B1x, B1 and B2) (Fig. 1) can be separated and quantified using weak anion exchange high-performance liquid chromatography [20, 23]. Current immunoassays for the determination of BALP in serum cannot distinguish between different BALP isoforms. The monoclonal antibodies used in these immunoassays have been reported to have different affinities for the two major BALP isoforms B1 and B2 [21]. Moreover, the calibrators used are characterized by significantly different proportions of BALP isoforms compared to each other, which increases the variability between methods [24, 25]. All four BALP isoforms are expressed in human bone tissue [10, 26] and in vascular smooth muscle cells (VSMC); that is, cells that play a key role in ectopic vascular calcification associated with increased serum BALP activity [7, 27]. All three BALP isoforms B/I, B1 and B2 are detected in the circulation, with B1 and B2 representing the highest activity [18, 28]. The B/I (bone/gut) isoform fraction is not a pure BALP isoform because it co-elutes with the circulating IALP isoenzyme, which contains approximately 70% BALP and 30% IALP [10, 29]. The B/I fraction represents only approximately 6% of the total BALP activity found in serum and is rarely of clinical significance, although extremely rare cases have been described [30]. The fourth BALP isoform, B1x, is less common in circulation and has so far only been detected in the serum of patients with chronic kidney disease (CKD) [31, 32, 33], with the highest activity found in patients undergoing dialysis [34].

BALP plays a key role in the propagation of tissue mineralization and is expressed in osteoblasts, chondrocytes, and other types of mineralizing cells such as calcifying VSMCs [23, 35] (Figure 2). Loss of functional mutations (mainly missense)

Step By Step Approach To Investigation Of Hypophosphatemia. Alp…

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