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Acute-Phase Proteins

Informations about header Acute-Phase Proteins
General Acute-phase proteins are plasma proteins involved in the response to inflammation, tissue injury or malignancy. During inflammatory processes, the plasma concentration of these acute-phase proteins will either increase (positive acute-phase proteins) or decrease (negative acute-phase proteins). Many positive acute-phase proteins are synthesised in the liver and are not elevated during functional disturbances or with stable chronic diseases.
Acute-phase proteins serve several different physiological functions for the immune system, some act to destroy or inhibit growth of microbes (e.g. C-reactive protein, mannose-binding protein, complement factors, ferritin, ceruloplasmin, serum amyloid A and haptoglobin), others provide negative feedback on the inflammatory response (e.g. serpins and alpha 2-macroglobulin). Acute-phase coagulation factors typically stimulate coagulation, this action may limit infection by trapping pathogens in local blood clots, in addition, some products of the coagulation system can contribute to the innate immune system by increasing vascular permeability and acting as chemotactic agents for phagocytic cells.
Elevated levels of positive acute-phase proteins are associated with bacterial infections, juvenile arthritis, tumours, Crohn’s disease, surgery, polymyalgia rheumatica, systemic vasculitis, burns and fractures.
Acute-phase proteins include: Alpha-1 acid glycoprotein, C-reactive protein (CRP), serum amyloid A, haptoglobin, ceruloplasmin, complement factors, ferritin and cytokines (e.g. Tumor Necrosis Factor (TNF-α), interleukin-1 beta, interleukin-6, interleukin-2, interleukin-8)
 

 

Albumin

 
    Specimen Reference range Dimension Method
ALBU24 Albumin in urine
urine 10 mL
   
PHO
    ALBU Albumin (U) >> Appendix  
< 20
mg/L  
    ALB24 Albumin (U) / 24h  
< 30
mg/24h  
ALB Albumin in serum >> Appendix
serum 1 mL
3200 - 4800
mg/dL
PHO
ALBP Albumin in puncture
puncture 1 mL
up to 1.5
g/dL
NEPH
ALBST Albumin in faeces
faeces 5 g
up to 9.2
μg/g St.
RID
ALBD Albumin in dialysate
dialysate 1 mL

see report

 
PHO
ALBF Albumin in amniotic fluid
amniotic fluid 1 mL

see report

 
NEPH
PALB Prealbumin
serum 1 mL
  till 4 Years 10 - 20
  from 4 Years 20 - 40
 
NEPH(2)
 
 
Informations about header Albumin
General Albumin (MW 66,000) is produced in the liver and has a half-life of approximately 20 days. Reduced serum albumin is associated with acute-phase response and chronic inflammation, urine albumin is an important prognostic indicator for kidney disease in diabetic patients, the measurement of albumin in CSF can be used to differentiate between cerebral disorders and infections.
 

 

Alkaline Phosphatase

Alkaline Phosphatase
    Specimen Reference range Dimension Method
AP Alkaline Phosphatase >> Appendix
serum 1 mL
male: till 31 Days 75 - 318
female: till 31 Days 48 - 408
male: till 1 Year 82 - 383
female: till 1 Year 124 - 341
male: till 3 Years 104 - 345
female: till 3 Years 108 - 317
male: till 6 Years 93 - 309
female: till 6 Years 98 - 327
male: till 9 Years 86 - 315
female: till 9 Years 69 - 325
male: till 12 Years 42 - 382
female: till 12 Years 51 - 332
male: till 15 Years 74 - 390
female: till 15 Years 50 - 182
male: till 18 Years 52 - 199
female: till 18 Years 47 - 171
male: from 18 Years 45 - 129
female: from 18 Years 45 - 129
U/L
PHO
APISO AP-Isoenzymes >> Appendix
serum 1 mL
     
    KNOAP Bone-AP >> Appendix  
  till 16 Years 62 - 100
female: from 16 Years < 74
male: from 16 Years < 75
%
GEL(1)
    LEBAP Liver-AP >> Appendix  
  till 16 Years < 31
female: from 16 Years < 72
male: from 16 Years < 71
%
GEL(1)
    DARMAP Intestinal-AP >> Appendix  
< 14
%
GEL(1)
    GALAP Bile-AP >> Appendix  
  till 16 Years < 7
female: from 16 Years < 14
male: from 16 Years < 9
%
GEL(1)
    MMAP Macro-AP >> Appendix  
< 1
%
GEL(1)
PLAP Placental Alkaline Phosphatase >> Appendix
serum 1 mL

see report

U/L
EIA(1)
 
 
 Alkaline Phosphatase
General Alkaline phosphatase (ALP) is an enzyme found in the liver; in Kupffer cells lining the biliary tract; and in bones (as enzymatic marker of the osteoblastic activity), intestines, and placenta. Additional sources of ALP include the proximal tubules of the kidneys, pulmonary alveolar cells, germ cells, vascular bed, lactating mammary glands, and granulocytes of circulating blood. ALP is referred to as alkaline because it functions optimally at a pH of 9.0. This test is most useful for determining the presence of liver or bone disease.
There are three genes for ALP - intestinal, placental and the liver/kidney/bone gene. The latter isoforms undergo post-translational modification with different carbohydrate sidechains being attached. In some instances it is important to be sure whether a raised plasma ALP is of liver or bone origin (e.g. malignancy, co-existing liver disease etc.).
 

 

Protein

The total protein fraction of plasma consists of >100 known proteins.

Albumin, a1-, a2- and a-globulins are synthesized in the liver, the proteins of
gamma-globulin by plasma cells.
 

Protein, total, in serum

LIS-code: GE
Indication: Increased ESR, proteinuria, edema, polyuria, chronic kidney and liver
diseases, diarrheas, trauma, shock, burn injuries, malnutrition.
Material: 1 ml serum
Method: enzymatic
TAT: 1 day
Dimension: g/dl
Ref.- range: 6.6 - 8.3
Note: standing: up to 10% protein concentration increase (orthostasis)

Erythrocyte Enzymes

Erythrocyte Enzymes
    Specimen Reference range Dimension Method
ACHE Acetylcholinesterase in EDTA blood
EDTA blood 2,7 mL
0.38 - 0.62
Delta pH
ENZ
GALK Galactokinase in EDTA blood >> Appendix
EDTA blood 2,7 mL
normal > 12
heterozygous 8 - 12
homozygous < 2
mU/g Hb
ENZ(2)
GAL1P Galactose-1-Phosphate in EDTA blood >> Appendix
EDTA blood 2,7 mL
7 - 22
μmol/L eryc.
ENZ(2)
G1PUT Galactose-1-Phospho-Uridyl-Transferase in EDTA blood >> Appendix
EDTA blood 2,7 mL
20 - 35
μmol/m/g Hb
ENZ(2)
G6PD Glucose-6-Phosphate-Dehydrogenase in EDTA blood >> Appendix
EDTA blood 2,7 mL
> 130
U/10^12 Ery
PHO(1)
GRD Glutathion Reductase in EDTA blood >> Appendix
EDTA blood 2,7 mL
5.0 - 11.0
U/g Hb
PHO(2)
HKE Hexokinase in EDTA blood >> Appendix
EDTA blood 2,7 mL
0.32 - 0.53
U/g Hb
EXT(2)
PGLUD Phosphogluconate Dehydrogenase in EDTA blood >> Appendix
EDTA blood 2,7 mL
5.1 - 10.4
U/g Hb
PHO(2)
PKE Pyruvatkinase in EDTA blood >> Appendix
EDTA blood 2,7 mL
5.3 - 17.3
U/g Hb
PHO(2)
TPMTS Thiopurin-S-Methyltransferase activity in EDTA blood. >> Appendix
EDTA blood 2,7 mL
normal > 20
heterozygous 10 - 20
homozygous < 10
nmol/gHb*h
HPLC(2)
TKL Transketolase in EDTA blood >> Appendix
EDTA blood 2,7 mL
42.0 - 69
60.0 - 85.0
U/L
EXT(2)
UDPGE UDP-Galactose-Epimerase in EDTA blood >> Appendix
EDTA blood 2,7 mL
19 - 35
μmol/h/g Hb
ENZ(2)
 

 

ADAMTS

ADAMTS
    Specimen Reference range Dimension Method
ADAAKT ADAMTS-13 activity
citrate blood 2 mL
40.0 - 130.0
%
EIA(2)
ADAAK ADAMTS-13 antibodies >> Appendix
citrate blood 2 mL
negative: < 12
borderline: 12 - 15
positive: > 15
U/mL
EIA(2)
ADAAG ADAMTS-13 antigen
citrate blood 2 mL
0.60 - 1.60
μg/mL
EIA(2)
 
 
Informations about header ADAMTS
General ADAMTS13 (a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13)—also known as von Willebrand factor-cleaving protease (VWFCP)—is a zinc-containing metalloprotease enzyme that cleaves von Willebrand factor (vWf), a large protein involved in blood clotting. It is secreted in blood and degrades large vWf multimers, decreasing their activity.
Genomically, ADAMTS13 shares many properties with the 19 member ADAMTS family, all of which are characterised by a protease domain (the part that performs the protein hydrolysis), an adjacent disintegrin domain and one or more thrombospondin domains.
Since the discovery of ADAMTS13, specific epitopes on its surface have been shown to be the target of inhibitory antibodies. Especially since the link between aortic valve stenosis and angiodysplasia was proven to be due to high shear stress (Heyde's syndrome), it has been accepted that increased exposure of vWf to ADAMTS13 due to various reasons would predispose to bleeding by causing increased degradation of vWf. This phenomenon is characterised by a form of von Willebrand disease (type 2a).
A large majority of thrombotic thrombocytopenic purpura (TTP) is associated with a severe deficiency of ADAMTS13. In most cases, ADAMTS13 severe deficiency is acquired via auto-antibodies to ADAMTS13; more rarely, ADAMTS13 deficiency is hereditary via ADAMTS13 gene mutations. ADAMTS13 auto-antibodies are either inhibitory of the catalytic activity or non inhibitory. ADAMTS13 mutations are spread all over the gene.
Diagnostic: A confirmation of a severe ADAMTS13-deficiency is specific for a classical TTP (HUS is not caused by a ADAMTS13 deficiency). Therefore ADAMTS13-antigen and ADAMTS13-activity have to be investigated. The differentiation between an aquired or hereditary TTP can be cleared by testing ADAMTS13 antibodies.